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  1. Mar 2024
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      Reply to the reviewers

      We would like to thank our reviewers for their constructive criticism and for their appreciation and enthusiasm for our study. Some reviewers expressed opposing views, particularly when it came to the function and identity of the Cdt1-related protein in Toxoplasma gondii. To avoid redundancy in our response, we would like to make a brief statement. Toxoplasma gondii and other apicomplexan parasites utilize unique and highly unusual modes of cell division; numerous studies suggest that multiple phases can run concurrently in apicomplexan cell cycles. The best-known examples include the asynchronous S/M cycles in schizogony and concurrent mitosis and budding in Toxoplasma endodyogeny. These overlapping phases are not a feature exclusive to apicomplexans, since in budding yeast, cytokinesis initiates in G1 phase by marking the location of budding on the surface of the mother. Based on years of previous research and from our experience, we adjusted our approach by focusing on the processes that are associated with each cell cycle phase rather than on their temporal order. While the model of a conventional cell cycle guides our studies, we “follow the breadcrumbs” that we discover and the published studies to create a more accurate model of apicomplexan cell cycle instead of relying on the traditional cell cycle map employed by distantly related eukaryotes. Below are point-to-point responses to reviewers’ comments.

      Reviewer #1 (Evidence, reproducibility and clarity (Required)):

      Summary: Hawkins et al. employ a reverse genetic approach to analyze the molecular function of the Toxoplasma gondii kinase Crk4 and the Toxoplasma gondii cyclin 4. The authors combine inducible depletion with imaging, (phospho-)proteomics, molecular modeling, and protein-protein interaction studies.

      Major comments: - The major conclusion of the manuscript is that TgCrk4/TgCyc4 regulate entry into mitosis and that the primary role of TgCrk4 is to suppress DNA re-replication and chromosome re-duplication (lines 105-106). The authors also provide evidence that TgCrk4 interacts with TgCdt1, a DNA licensing factor ("TgCdt1" is missing in line 107). (had been corrected) By sequence homology, the authors found homologues of TgCrk4 only in apicomplexan parasites with binary division and concluded that the dominant division mode, presumably schizogony, is repressed in these organisms in favor of binary division. Indeed, internal budding and daughter cell formation is defective in the inducible depletion mutants of TgCrk4 and most experiments focus on this developmental stage. However, the analysis of preceding events, such as DNA replication is rather brief. If G2 is indeed regulated by TgCrk4/TgCyc4, one would assume that the parasites are post-S phase and the nucleus contains two copies of the genome, as indicated in Fig. 2C. The data shown in Fig. 3H and 7A, however, show that the TgCrk4 and TgCTD1 depletion induces a developmental arrest pre-S phase. This contradicts the main conclusions of the manuscript.

      *We agree that the G2 location is odd for a conventional cell cycle model. Given the high possibility that cell cycle phases can overlap in apicomplexans, we determined the relative position of G2 phase in Toxoplasma endodyogeny by instead focusing solely on the processes that are attributed to a specific cell cycle phase (such as DNA replication for S phase, DNA re-replication for G2 phase, DNA segregation for mitosis). Our approach shows that Toxoplasma G2/M checkpoint operates upstream of SAC, which led to enrichment of parasites with replicated DNA (Fig. 3H and Fig. 7A), which places G2 at the end of S-phase. Our focus in the present study is on the G2 functions, the control of centrosome and chromosome reduplication, but we appreciate the suggestion to examine DNA replication in Toxoplasma, which could be investigated in future studies. *

      Indeed, many data of this manuscript could support an alternative conclusion, i.e., that TgCrk4 regulates entry into S-phase (similar to Plasmodium falciparum Crk4: PMID: 28211852). This alternative conclusion is supported by the data showing that TgCyc4 is in the nucleus during S-phase (Fig. 1H) and that TgCrk4 interacts with TgCdt1, which has a well-known role in origin of replication licensing and loading of the MCM complex. MCM subunits were less phosphorylated in absence of TgCrk4, which could also suggest a role for TgCrk4 in S phase. Together, it seems more parsimonious to interpret the data as a DNA replication phenotype rather than a phenotype in G2.

      *We understand some confusion from prior data, but PfCrk4 is not orthologous to TgCrk4 (Alvarez & Suvorova, 2017); The true TgCrk4 ortholog had not been found in Plasmodium genomes. Our understanding is that nuclear accumulation of TgCyc4 in S-phase activates TgCrk4, which leads to repression of the DNA reduplication. One of the possible mechanisms involves interfering with loading of the MCM complex on chromatin mediated by hyper-phosphorylated TgiRD1 (former TgCdt1), which has been reported in other eukaryotes. We also believe that increased MCM phosphorylation indicates entry into or active S-phase, while the reduced phosphorylation that was detected in Crk4-depleted cells supports a block at the end of S-phase (G2). *

      • *

      The currently provided data on the DNA content are, however, clearly insufficient to draw firm conclusions. The gating strategy (dotted lines in Figs. 3H, 7A) is unclear. Why are populations, e.g., not separated at the lowest part of the depression in the histogram, but shifted towards lower DNA content? This seems to overestimate the percentage of cells that have a higher DNA content and the statement in lines 269-271, i.e., that TgCrk4 deficient parasites break the "once and only once" rule, is not supported by data.

      *We corrected the gating of the FACScan plots to separate G1, S, G2+M, and parasites with over-duplicated DNA. Please note that, in general, the cell cycle gating of FACScan data is relative and somewhat subjective when it comes to the gaussian curve. Independent of the chosen gates, our data show that removal of either TgCrk4 or TgiRD1 led to substantial decrease of the G1 population (reduction of 1N peak) accompanied by increase of parasites in the process of replication, completed replication (increase of 1.8 N peak), as well as undergoing DNA re-replication, which supports our claim in lines 269-271. In the case of TgiRD1, the number of parasites with re-duplicated DNA nearly doubled upon 8h of factor deficiency. *

      • *

      It is also unclear how may biological replicates are represented by these data (Figs. 3H, 7A), a critical wild type control at t = 4 h is missing, as well as a statistical analysis. Alternatively, the authors could use microscopy to quantify the DNA content of individual nuclei, which would yield a direct read out on whether a nucleus is in pre-S phase, S-phase or post-S phase. Defining the onset of S-phase indirectly by the number of centrosomes per cell seems imprecise, given the small size of the structure and the resolution of the microscope. Without solving these issues, the major conclusions and several minor statements throughout the manuscript are in question.

      *Thank you for your point, we performed a minimum of three independent experiments to evaluate the DNA content of TgCrk4- or TgiRD1- (former TgCdt1) depleted tachyzoites and have now indicated this in the figure legends. The 0h time point is a “wild type” control, since the parasites that expressed factors were incubated without auxin (mock treated) for 4h. The DNA content of Toxoplasma has been thoroughly studied and we are thus confident our 0h data is a good representation of asynchronous healthy populations. Although the parental strain had been examined, due to the data density mentioned in the reviews, we included only relative results (control and two experimental points) for clarity. Our concern with using microscopy to analyze DNA content is that it can be highly subjective, hinging on the quality of staining and imaging, while flow cytometry produces more unbiased datasets. We have considered the concern that the start of centrosome duplication can be difficult to identify, but the centrin-positive centrosomes move apart by the middle of S-phase. The independent structures are then distinct and easy to resolve, providing a popular means of marking G1/S transition in Toxoplasma. *

      • Lines 187-189: The mentioned checkpoint is unclear and so is the "specific cell cycle population". Fig. 2B analyses budding, but as the final step in the cell cycle, the knock down parasites may have arrested at various other stages of the cell cycle. In addition, it is unclear on which primary data Fig. 2B is based. It appears these may be at least partially shown in Fig. 3. If so, please reorganize as this is highly misleading.

      *“A checkpoint” in the indicated lines refers to G2/M and SAC, which are regulated by TgCrk4 and TgCrk6, respectively. We refer to “specific cell cycle population” since each transgenic parasite that is subject to G2/M or SAC arrest can allow us to isolate very different cell cycle stages. TgCrk6-dependent arrest had been confirmed by the presence of unresolved centrocone (not shown but was previously reported in Hawkins et al., 2022), while we thoroughly examined the novel TgCrk4-dependent block by focusing on many parameters, such as joint centrosomes, single-bud assembly, or unresolved apicoplast. Fig. 2 and Fig. S2 summarize our rigorous quantifications of these phenotypes. For convenience, we used budding efficiency as a readout to compare arrest and release of G2/M and SAC, which was incorporated in Fig. 2B. Table S4 contains the primary data used in all figures in the manuscript, including Fig. 2B. *

      • Line 246-254: It is unclear how many biological replicates were performed and how many cells were analyzed to conclude that TgCrk4 deficient parasites cannot form a bipolar spindle (Fig. 2H, S3B). This, together with the possibility that the developmental arrest occurs pre-S phase (Fig. 3H), does not support the statement, that the G2/M transition is regulated by the novel TgCrk4-TgCyc4 complex.

      We have indicated our replicates in the M&M. As addressed for Fig. 3H above, these IFA experiments were performed in at least three independent experiments.

      * * Minor comments: - Throughout the manuscript, please reorganize and present the figures in order of appearance in the text. Also, Fig. 1G summarizes data that are only presented in Fig. 1H. Please reorder. Similarly, Fig. 2C appears to summarize data that are only presented later.

      *Thank you for the suggestion, however we must abide by the standards of the publishers. The order of the figures must be maintained, but there is a substantial degree of freedom in organizing panels within figures. Fig. 1G summarizes data shown in Fig. 1F, H, while Fig. 2C summarizes many panels including preceding Fig. 2B and Fig. S2. Most of our schematics are placed at the top of figures to provide guidance for the relevant experiments. *

      • Why was only the "G1" timepoint quantified in Fig. 1H? Do the other images shown in F and H represent the majority of cells analyzed?

      *You are correct, we indicated the percentage of factor-positive parasites only when the factor emerges during a specific cell cycle phase. For example, the TgCyc4-positive parasites with 1 centrin dot were quantified to show that TgCyc4 emerges in the middle of G1 phase. The lack of a number indicates that the image represents all the parasites progressing through this phase; we have added this explanation to the figure legends. *

      • Several micrographs lack scale bars (Fig. 1B, D; 2E, F, H, I; 6D; 7F, H and S2G, S3A, B; S5A, B, D).

      *Thank you, we have added the scale bars to indicated images.

      *

      • Lines 83-85 and 93-95: Recently several publications investigated the cell cycle of the apicomplexan parasite Plasmodium and data are accumulating, showing that there may be a gap between the last S phase and segmentation (e.g., PMID: 35731838; PMID: 35353560), which may be interpreted as a G2 phase. Thus, these statements could be revised to reflect the current literature.

      *The studies mentioned provide very valuable insights into S-phase dynamics; the gap that was detected between S-phase and segmentation includes mitotic events such as prophase, metaphase, and anaphase prior to telophase (karyokinesis to segmentation). However, studies using means like stage-specific markers could help resolve the composition and order of events in the apicomplexan cell cycle. We used processes specific to G2 (repression of DNA and centrosome reduplication) and identified TgCrk4/TgCyc4 as the first G2 markers in apicomplexans. *

      • Fig. 4 shows the effect on protein abundance and phosphorylation upon TgCrk4 depletion. Fig. 4B seems somewhat redundant as a more detailed analysis with two timepoints is shown in the rest of the figure.

      *Fig. 4B is provided in contrast to the plot in Fig. 4A. It demonstrates that TgCrk4 depletion results in a far more pronounced effect on global phosphorylation rather than on proteolysis. While Fig. 4B highlights the checkpoint arrest, panels C and D are dedicated to the search for TgCrk4 substrates: the phospho-sites that immediately lost intensity of phosphorylation and remained low during the 4h block. *

      *

      *

      • Lines 146-148: This statement is confusing in light of the expression data in Fig.1 F and H. If they stabilize each other, how is TgCrk4 stabilized in G1, when TgCyc4 is absent?

      We believe that multiple mechanisms contribute to the stability and function of TgCrk4. We tested one and found that depleting the cyclin partner led to reduced expression of TgCrk4, and were able to conclude that the complex is stable when both subunits are expressed. Please note that we probed the mixed cell cycle populations by WB, and our proteomics data show that TgCrk4 interacts with many partners (Fig. 1E). Thus, it is likely that G1 stability may have been mediated by other partners, or by a higher transcription/translation rate, which could be evaluated in further experiments that focus on the regulation of TgCrk4/TgCyc4 complex.

      • *

      • Fig. 2D, and G: Please provide representative images of what has been quantified, as E/F and H/I are apparently UxEM images.

      The corresponding images are included in Fig. S2.

      • Line 236-243: This statement seems to be based on a single IFA shown in Fig. 2K. If so, the manuscript would benefit from clearly stating that this is a singular observation.

      *Thank you, we have provided clarification as described in previous points. *

      *

      *

      • Lines 301-304: In the cited publication, the TgOTUD3A knockout could not be complemented, which raises the possibility that other factors are involved. Thus, this statement would benefit from revision.

      *The lack of TgOTUD3A KO complementation is an example of the unappreciated complexity of apicomplexan cell cycle regulation by controlled proteolysis. We highlighted the similarity of TgCrk4 and TgOTUD3A deficiencies, which indirectly confirms their partnerships in the G2 network. Fig. 8A shows that, in addition to TgOTUD3A, the G2 network contains numerous factors. *

      *

      *

      • Lines 421-422: PfCdt1 was annotated in PlasmoDB some time ago and this statement needs to be revised.

      *Please see our response to comments made by Reviewer 2. Briefly, we agree with Reviewer 2 comment that TgCdt1 does not function as conventional DNA replication licensing factor CDT1. Therefore, we named TGME49_247040 TgiRD1 – inhibitor of DNA and centrosome ReDuplication 1. *

      • *

      • Lines 448-450 and Fig. 6F: Are these data from a single biological replicate and how many cells were analyzed for the different time points? Given the insufficient data on the DNA content, the paper would benefit form more conservative conclusions on the role of TgCdt1. The numbers of biological replicates were added throughout the text, also please refer to our response to Reviewer 2 and the comment above.

      Reviewer #1 (Significance (Required)):

      • This manuscript investigates the role of TgCrk3, TgCyc4 and TgCdt1s and provides a large amount of data.
      • These data will contribute to our understanding of the unusual division modes of Apicomplexa, a field of research that recently gained momentum.
      • These data will be interesting to the community of cell and molecular biologist, which work on the fundamental biology of eukaryotic microorganisms.
      • My field of expertise is the cell biology of Apicomplexa.

      Reviewer #2 (Evidence, reproducibility and clarity (Required)):

      Summary: In this Manuscript, Hawkins et. al. describe advances in the apicomplexan parasite cell cycle, which is reminiscent but distinct from mammalian cell cycle regulation. These differences include a presumed lack of G2 phase and the ability to replicate in either a multinuclear (schizogony) or binary (endodyogeny) manner. Using Toxoplasma gondii (TG) as a model, the authors seek to expand the current understanding of how these highly variable parasitic cell cycles are regulated by describing a previously unreported G2 phase. Building on the authors earlier work, this manuscript defines the function of TgCrk4 and identifies a novel binding partner, TgCyc4. Crk4 and Cyc4 control a G2/M checkpoint by regulating centrosome duplication and separation.

      The authors also identify 247040, a protein with previously no known function, as a binding partner and substrate of TgCrk4/TgCyc4 and several replication fork proteins such as MCM and PCNA. Results indicate that the protein negatively regulates replication and centrosome duplication. The authors propose to rename this protein TgCDT1 despite "low sequence similarity" and having a completely opposite function to eukaryotic CDT1. Using Swiss-Prot modeling the authors claim 247040 bears a "partial resemblance" to mammalian CDT1. Indeed, both of these proteins show high intrinsic disorder and have 2 folded domains. While 247040, like hCDT1, does contain cyclin interacting motifs (Cy), a collection degrons (not all shared with other CDT1 orthologs), and an NLS, the list of nuclear cell cycle proteins that also contain Cy and degron motifs would be very long. Further, 247040 is regulated in an opposite manner to all other CDT1 orthologs because it is absent in TG G1 and present in TG S phase; eukaryotic CDT1 is either degraded or relocalized to the cytoplasm in S phase, and evidence for degradation via APC/C is minimal. Crucially, loss of 247040 resulted in inappropriate replication ("re-replication"), whereas all other eukaryotic CDT1 orthologs are essential for replication. Re-replication in eukaryotic cells can be caused by excess or hyper-active CDT1, not by loss of CDT1 activity as shown here for 247040. Clearly 247040 is a negative regulator of DNA replication, and as such, is not a candidate for the TgCDT1 ortholog. If anything, it is functionally analogous to metazoan geminin, the negative regulator of metazoan CDT1; of note, geminin also has centrosome-related phenotypes. We cannot support naming 247040 TgCDT1 because it will cause confusion in the field.

      Aside from this major issue, the study is well-executed, rigorous, quantitative, and thorough; it has many strengths from the unbiased interaction screens. The authors' sequence analysis also suggests broader possibilities for cyclin structures than had previously been appreciated. We appreciate the legend in Figure 2 to the organism-specific terminology.

      Major comments: The spatiotemporal dynamics of 247040, its role in repressing TG DNA replication, lack of PIP motif and winged helix domain indicate that some other nomenclature, other than TgCdt1 will be a better name for this protein of previous unknown function.

      We would like to thank Reviewer 2 for this highly insightful comment. We agree that TGME49_247040 functions as a CDT1 inhibitor rather than as CDT1 itself, so conserving the name would produce confusion in the cell cycle field. Based on TGME49_247040 protein function we decided to name this factor TgiRD1 – inhibitor of DNA and centrosome ReDuplication 1. We revisited our data, looked deeper into the protein structure, and adjusted our conclusions. Our new Figure S5 shows differences in the predicted folding of HsCDT1 and TgiRD1. We could not ignore the fact that TgiRD1 is phylogenetically related to CDT1 in ancestral branches and metazoans (Fig. 6B), but we identified substantial differences that may indicate a selective loss (or inheritance) of protein features. For example, TgiRD1 does not interact with ORCs that are critical for the licensing step, but TgiRD1 retained an MCM binding domain (winged helix-turn-helix) that plays a role in licensing and firing. Rather than CRL4Cdt2 degrons, TgiRD1 contains APC/C degrons that would be activated late in mitosis (similar to regulation of Geminin). Together with the lack of DNA licensing control in G1 and its opposing expression profile, we concluded that TgiRD1 represents a Cdt1-related protein that controls DNA and centrosome reduplication in S and G2 phases.

      Minor comments:

      1. For clarity, please include the number of replicates in the figure legends where appropriate. We added the requested information.

      For microscopy/imaging, how were representative cells/images chosen? The representative images constituted the most common phenotype of the feature we aimed to highlight, and most are accompanied by quantifications.

      In addition to the ELM analysis, the authors could also employ fold recognition software (such as Promal) to analyze 247040 structural models to show similarity to known protein structures.

      We use a variety of folding prediction software, including AlphaFold2, PyMol, and template-based SWISS-PRO module to examine protein structures in our study, indicated in the text and figure legends. Our new TgiRD1 (former TgCdt1) analysis is based on an AlphaFold2 prediction (Fig. S5). All the software we used is listed in the M&M section.

      Line 107: missing words "TgCdt1"

      *We corrected the sentence.

      *

      Line 141: the interpretation that the C terminus is "unstable" is misleading if it is simply that the protein cannot tolerate a fusion to the C-terminus.

      *We successfully incorporated a tag at the C-terminus (confirmed by sequencing across the recombinant gene) but could not detect protein expression. If our protein could not tolerate a recombinant tag, the transgenic parasites would not survive because TgCyc4 is essential protein. Therefore, since the parasites survived, we concluded that the lack of TgCyc4-AID-HA expression was due to native truncation at the C-tail (instability). *

      Line 221: word choice "reminisced" We have changed the wording.

      Line 348 refers to Orc4 expression in Figure 4A, but the data point is not labelled. Fig. 4A references GO group (DNA replication/licensing factors), and the raw data is included in Table S6, which is now indicated in the text.

      Lines 407-8 and 510-11: Reference Fig 1E We added the reference.

      Line 408: please define what is meant by "dominant interactor" We meant that TgiRD1 is the most prominent interactor of TgCrk4 and TgCyc4. To clarify the confusion, we changed the wording to “primary interactor”.

      Reviewer #2 (Significance (Required)):

      This manuscript makes great strides in defining apicomplexan cell cycle control and genome replication. These strides include defining a previously unrecognized G2/M checkpoint controlled by TgCrk4 and the novel TgCyc4. Further, the authors identify a binding partner and substrate of the novel Crk4/Cyc4 kinase complex, 247040 that acts as a repressor of replication.

      Reviewer #3 (Evidence, reproducibility and clarity (Required)):

      Summary The present study Hawkins et al have described the important role of Cyclin-CDK complex in an apicomplexan parasite Toxoplasma(Tg) which exhibit binary mode of cell division like many other eukaryotes. In the apicomplexan field it is generally shown that G2 phase of cel cycle is either absent or has very little role. The authors here demonstrate that the combination of Tg CRK4 and Tg Cyclin4 works during the G2 phase of cell cycle such as chromosome rereplication and centrosome reduplication. In order to show the function of Cyclin-CRK function they used Auxin degradation system to down regulate or deplete the protein and study parasite growth during cell cycle as well as they used tagged parasite to identify the protein complex with these two molecules. In the study they showed that these two molecules Cyc4 and cRK4 formed the complex in protein pulldown method and show identical function in the cell cycle. In addition to thiese two proteins they also found another interacting partner Cdt1 that was further analysed to be involved in controlling Chromosome rereplication and centrosome. So overall the study is nicely performed and three molecules of Cyclin4-CRk4-Cdt1 and their role is illustrated in the binary mode of cell division in Toxoplasma.

      Comments 1.Though no new experiments need to be performed but it will be good if some details are given as to which stage of tachyzoite cycle the protein complex were performed and if there is difference in the various phases of cell cycle especially the s phase and the M phase. Are these period changed. Since G2 is suppose to be absent in many apicomplexan do the authors suggest that G2 phase is only coupled to binary mode of cell division. Please discuss how it is then linked to the other part of cell cycle.

      *You are correct, we propose that the presence of G2 phase is linked to binary division in apicomplexans and our hypothesis is supported by the overall evolution of the cell cycle (see Discussion section). We also entertained the hypothesis that G2 operates in multinuclear division since all apicomplexans encode TgiRD1 orthologs (please, see the Discussion section). For the first time, we identified the major functions of G2 functions (repression of the DNA and centrosome reduplication) in the apicomplexan cell cycle. However, given the unresolved organization of the Toxoplasma (or any apicomplexan) cell cycle, it is currently impossible to define the boundaries of G2. According to our study, TgCrk4 and TgCyc4 control G2/M transition or the end of G2 phase, and we still lack markers of G2 entry. In our comparative synchronization study (Fig 2), we uncovered the temporal link between G2/M and SAC regulatory points, which is discussed in the results section. *

      Ganter et al have studied CRK4 in Plasmodium previously and they do find in their phosphoproteome study the similar association with the DNA replication machinery with CRK4 but no cyclin was identified in their study. In the cyclin study by Roques et al it has been shown that no cell cycle cyclins are found in Apicomplexan so can the author discuss more how these complex can be different in two apicomplexan species. They describe that Crk4 is novel cell cycle kinase though this has been studied earlier. Authors have almost not discussed these previous finding with respect to their in this study.

      *We would like to clarify this confusion. We have not discussed Ganter et al. studies because PfCRK4 is not orthologous to TgCrk4, but rather it is related to TgCrk6. Unfortunately, the Plasmodium and Toxoplasma Crk nomenclature was published almost concurrently. Our previous (Alvarez & Suvorova, 2017) and current study show that Plasmodium and other apicomplexans that divide by multinuclear division do not encode TgCrk4 orthologs (and/or TgCyc4). Additionally, the mentioned studies by Roques and Ganter were released prior to newer genome annotations that include additional cyclin-domain proteins, including 10 Toxoplasma cyclins (5 new) that we categorized in our recent publication (Hawkins et al., 2022). Although the newly annotated cyclins are not related to conventional cell cycle cyclins, we had proven empirically that TgCyc1 together with TgCrk6 controls SAC, and now, the specific interaction of TgCyc4 with TgCrk4 controls G2 processes. Lastly, we call TgCrk4 “a novel” kinase only in the meaning that it is a novel cyclin-dependent kinase that is not related to known CDKs in other eukaryotes. The identification of TgCrk4 in our previous study (Alvarez & Suvorova, 2017) is described in the Introduction section and at the opening of the Results. *

      The manuscript is too dense, in terms of both figures and text. At times loses the focus and hence can be organised with most important finding in the figure and text. Especially Fig2, Fig4 and Fig7. Fig5 does not give too much in terms of the real finding an in fact take away from the focus. Some parts of these figures can be simplified or moved to supplementary. Some of the figures in Fig2 and 7 are missing the scale bars.

      We respectfully disagree with some conclusions made by the Reviewer. Our study contains ample material that is intended to guide the reader through the complexity of the Toxoplasma cell cycle and the intricate structures contained in the parasite. We have also introduced a few novel approaches that require additional schematics and dedicated discussions.

      • Fig 2*. The G2/M block, as well as the G2 phase, had never been detected in apicomplexans. We created a new approach to determine the timing of the G2/M checkpoint, which involves comparison to a known cell cycle block. Panels A, B, and C provide visuals and summarize our findings. The main events are highlighted with arrows (Panel C), while graphs (panel B) show differences in responses. The rest of the figure is devoted to quantification of the primary events caused by TgCrk4 deficiency, since the G2 block had never been examined. While the U-ExM images of the entire vacuole (2-4 parasites) may seem overwhelming, they represent that the deficiency is consistent. *
      • Fig 7* is devoted to the major Crk4/Cyc4 interactor TgiRD1 (former TgCdt1). This is one of the first mechanistic studies of central cell cycle regulators in Toxoplasma. This Cdt1-related protein was examined at the molecular level to support the main claims of its control of G2 Nevertheless, we moved two panels from Fig. 7 into the supplement. *
      • 4* is organized as follows. Top row: panels A, B visualize the G2/M checkpoint block at the protein level. Middle row: panels C, D, and E represent the workflow to find TgCrk4 substrates. Bottom row: panels F, G highlight TgCrk4 substrates of interest that are discussed in the paper. *
      • 5* is an in-depth analysis of the central cell cycle regulators across Apicomplexa phylum, a key figure of the study. Its comparative nature supports our main message: binary division is regulated by TgCrk4/TgCyc4, which are only expressed in a subgroup of apicomplexans that divide in a binary mode. *

      May be bit more discussion of ORC in relation to their Cyclin-CRK complex as they did find upregulation of the ORC in their genome profiling. So may be instead of CDT1 these are more important in the licencing of DNA replication.

      *Our choice to focus on Cdt1-related protein was driven by the fact this protein is a major component of the TgCrk4/TgCyc4 complex, while the ORCs act downstream (as TgCrk4 substrates). Shifting focus to ORCs opens an entire new project, which will be explored in the future. *

      5 The model in Fig8B does not take Cyc4 into consideration and I feel is bit oversimplified as there are many factors that may be responsible for centrosome non separation. The S and G2 are no separated in the Cell cycle as given in this Fig.

      Referring to comment 3, we focused on empirically supported, central findings and created the first model of centrosome cycle regulation in T. gondii. We intentionally drew focus to TgCrk4, which was extensively studied, while TgCyc4 received less attention due to difficulties in modulating its expression. We have used transcriptional downregulation to evaluate TgCyc4 (tet-OFF model), which is unfavorable for cell cycle studies because it exceeds the duration of the cell cycle. The unclear cell cycle borders are addressed in the introduction to this response. Briefly, the organization of apicomplexan cell cycle is currently unclear, thus most of the schematics are approximate.

      It is not clear from the data with CDt1 if this linking the inner and outer centrocone or its down regulation breaks the bipartite centrosome. May be some reflection it will be useful.

      *Our model suggests that both TgCrk4 and TgiRD1 (former TgCdt1) affect only the inner core of the centrosome, which we propose is comprised of two types of linkers. The arrows in Fig. 8 point specifically to the linkers whose stability depends on the expression of TgCrk4 or TgiRD1. *

      Minor comments

      I what is SAINT analysis as it is not described in methods.

      *We added the description of our SAINT analysis to M&M.

      *

      How was budding quantified

      *We supplemented the figure legend with the required information. *

      Western blot can have predicted size

      *Due to density of the figures, we did not supply the predicted MW of the proteins when they display the proper PAGE motility. *

      what does red star mean in Blot 1C

      *We added the description to the figure legend.

      *

      What does the number in Fig1H means please explain in the legends and same for Fig6F. In fig 1, removing the inhibition for 5 hours led to very less budding, but in fig 3, removing inhibition showed increased budding (50% in 2 hours). Please explain

      *Please see our response to the reviewer 1 minor comment regarding Fig. 1H and 6F. *

      *We presume that there is some confusion regarding figure numbers. Perhaps the Reviewer refers to Fig. 2B. Indeed, the 4h block at G2/M led to reduced budding (Fig. 2B), while release from the block for 2 hours (Fig. 3C, post-recovery) allows parasites to continue cell cycle progression and reach the next stage –budding. The numbers over the Fig. 3A, B, and C panels are from the plots in Fig. 2B to help give a comprehensive representation of the analyzed timepoint. *

      Fig2 has no scale bars -please add- this figure is too dense. May be fig2A, B,C can be in supplementary, legend in the figure can be in the figure legend.

      Please see our response to comment 3. We have included scale bars.

      Also this figure2 H and I in not quoted in line 231. Also this figure2 has no panel J but goes directly from I to K

      *The alphabetical order was corrected, and the reference added. *

      Fig3 the FigG can be more relevant in the Figure 8 while describing about the Crk4 and Cyc4 and CDt1 in binary mode of cell division. Also please define what stars mean either in legend or methods section in terms of significance.

      *Thank you for the suggestion. The Fig. 3G schematics summarize the overall findings of the Figure and acts as an intermediate conclusion in this study. We added the meaning of the stars in the M&M section. *

      Line 107 the sentence is incomplete

      We have corrected the sentence.

      Line 217 may be the figure could be referred as then it is not cleat about the description.

      Due to the density of the figures and well-established dynamics of the centrocone and basal rings, we included the reference to a publication rather than as a figure panel.

      **Referees cross-commenting**

      The study is quite rigrous and with analyses of CRK4-CYC4 and CDT. However it will be better if authors please revisit their conclusions on G2 phase of cell cycle in Toxoplasma based on their findings. The study will have important bearing on the community studying apicomplexan parasites and DNA replication as well as who work on eukaryotic cell cycle.

      Reviewer #3 (Significance (Required)):

      Significance In the manuscript by Hawkins etal have illustrated that in the apicomplexan parasite that have binary mode of cell division present a Cyclin-Crk complex with detailed analysis of Tg Crk4-Cyc4 that are novel in these group pf parasite infect humans and animal alike like malaria parasite and ones affecting cattle and chicken. So these finding are novel as very little is known about this interaction. The significant finding is to show how the G2 phase of cell cycle may be regulated in these parasites and how DNA licencing factor Cdt1 is highly divergent but part of this CRK-Cyclin complex.

      So though it discusses more on the Toxoplasma but it may be of interest to the scientist working on eukaryotes with divergent mode of cell cycle.

      General Assessment - The findings are novel but the manuscript is too dense and at time loses the focus. May be both text and Figures could be made less dense so that important finding are revealed in better way.

      Advance - It does give important insight into the cell cycle in apicomplexan parasite and how even though there are no cell cycle cyclin in Apicomplexa. The findings here suggest how different complexes can substitute for the function. It does extend the knowledge in the field of Cell division in divergent parasites both in terms of mechanistic, functional and technical way.

  2. Feb 2024
    1. Author Response

      The following is the authors’ response to the original reviews.

      Public Reviews:

      Reviewer #1:

      Summary:

      In this study, Yan et al. investigate the molecular bases underlying mating type recognition in Tetrahymena thermophila. This model protist possesses a total of 7 mating types/sexes and mating occurs only between individuals expressing different mating types. The authors aimed to characterize the function of mating type proteins (MTA and MTB) in the process of self- and non-self recognition, using a combination of elegant phenotypic assays, protein studies, and imaging. They showed that the presence of MTA and MTB in the same cell is required for the expression of concavalin-A receptors and for tip transformation - two processes that are characteristic of the costimulation phase that precedes cell fusion. Using protein studies, the authors identify a set of additional proteins of varied functions that interact with MTA and MTB and are likely responsible for the downstream signaling processes required for mating. This is a description of a fascinating self- and non-self-recognition system and, as the authors point out, it is a rare example of a system with numerous mating types/sexes. This work opens the door for the further understanding of the molecular bases and evolution of these complex recognition systems within and outside protists.

      The results shown in this study point to the unequivocal requirement of MTA and MTB proteins for mating. Nevertheless, some of the conclusions regarding the mode of functioning of these proteins are not fully supported and require additional investigation.

      Strengths:

      (1) The authors have established a set of very useful knock-out and reporter lines for MT proteins and extensively used them in sophisticated and well-designed phenotypic assays that allowed them to test the role of these proteins in vivo.

      (2) Despite their apparent low abundance, the authors took advantage of a varied set of protein isolation and characterization techniques to pinpoint the localization of MT proteins to the cell membrane, and their interaction with multiple other proteins that could be downstream effectors. This opens the door for the future characterization of these proteins and further elucidation of the mating type recognition cascade.

      Weaknesses:

      The manuscript is structured and written in a very clear and easy-to-follow manner. However, several conclusions and discussion points fall short of highlighting possible models and mechanisms through which MT proteins control mating type recognition:

      (1) The authors dismiss the possibility of a "simple receptor-ligand system", even though the data does not exclude this possibility. The model presented in Figure 2 S1, and on which the authors based their hypothesis, assumes the independence of MTA and MTB proteins in the generation of the intracellular cascade. However, the results presented in Figure 2 show that both proteins are required to be active in the same cell. Coupled with the fact that MTA and MTB proteins interact, this is compatible with a model where MTA would be a ligand and MTB a receptor (or vice-versa), and could thus form a receptor-ligand complex that could potentially be activated by a non-cognate MTA-MTB receptor-ligand complex, leading to an intracellular cascade mediated by the identified MRC proteins. As it stands, it is not clear what is the proposed working model, and it would be very beneficial for the reader for this to be clarified by having the point of view of the authors on this or other types of models.

      We are very grateful that Reviewer #1 proposed the possibility that MTA and MTB form a receptor-ligand complex in which one acting as the ligand and the other as the receptor. We considered this hypothesis when asking how dose MTRC function, too. However, our current results do not support this idea. For instance, if MTA were a ligand and MTB a receptor, we would expect a mating signal upon treatment with MTAxc protein, but not with MTBxc. Contrary to this expectation, our experiments revealed that both MTAxc and MTBxc exhibit very similar effects (Figure 5, green and blue), and their combined treatment produces a stronger effect (Figure 5, teal). This suggests a mixed function for both proteins. (We incorporated this discussion into the revised version [line 120-121, 240-244].) It is pity that our current knowledge does not provide a detailed molecular mechanism for this intricate system. We are actively investigating the protein structures of MTA, MTB, and the entire MTRC, hoping to gain deeper insights into the molecular functions of MTA and MTB.

      Additionally, we also realized that the expression we used in the previous version, “simple receptor-ligand model”, is not clearly defined. As Reviewer #1 pointed out, in this section, we examined whether the individual proteins of MTA and MTB act as a couple of receptor and ligand. We think this is the simplest possibility as a null hypothesis for Tetrahymena mating-type recognition. We have clarified it in the revised version (line 90-91, 104-106). According to this section, we proposed that MTA and MTB may form a complex that serves as a recognizer (functioning as both ligand and receptor) (line 117-118).

      (2) The presence of MTA/MTB proteins is required for costimulation (Figure 2), and supplementation with non-cognate extracellular fragments of these proteins (MTAxc, or MTBxc) is a positive stimulator of pairing. However, alone, these fragments do not have the ability to induce costimulation (Figure 5). Based on the results in Figures 5 and 6 the authors suggest that MT proteins mediate both self and non-self recognition. Why do MTAxc and MTBxc not induce costimulation alone? Are any other components required? How to reconcile this with the results of Figure 2? A more in-depth interpretation of these results would be very helpful, since these questions remain unanswered, making it difficult for the reader to extract a clear hypothesis on how MT proteins mediate self- and non-self-recognition.

      Several factors could contribute to the inability of MTA/Bxc to induce costimulation. It is highly likely that additional components are necessary, given that MTA/B form a protein complex with other proteins. Moreover, the expression of MTA/Bxc in insect cells, compared with Tetrahymena, might result in differences in post-translational modifications. Additionally, there are variations in protein conditions; on the Tetrahymena membrane, these proteins are arranged regularly and concentrated in a small area, while MTA/Bxc is randomly dispersed in the medium. The former condition could be more efficient. If there is a threshold required to stimulate a costimulation marker, MTA/Bxc may fail to meet this requirement. Much more studies are needed to fully answer this question. We acknowledged this limitation in the revised version (line 244-248).

      Reviewer #2:

      This manuscript reports the discovery and analysis of a large protein complex that controls mating type and sexual reproduction of the model ciliate Tetrahymena thermophila. In contrast to many organisms that have two mating types or two sexes, Tetrahymena is multi-sexual with 7 distinct mating types. Previous studies identified the mating type locus, which encodes two transmembrane proteins called MTA and MTB that determine the specificity of mating type interactions. In this study, mutants are generated in the MTA and MTB genes and mutant isolates are studied for mating properties. Cells missing either MTA or MTB failed to co-stimulate wild-type cells of different mating types. Moreover, a mixture of mutants lacking MTA or MTB also failed to stimulate. These observations support the conclusion that MTA and MTB may form a complex that directs mating-type identity. To address this, the proteins were epitope-tagged and subjected to IP-MS analysis. This revealed that MTA and MTB are in a physical complex, and also revealed a series of 6 other proteins (MRC1-6) that together with MTA/B form the mating type recognition complex (MTRC). All 8 proteins feature predicted transmembrane domains, three feature GFR domains, and two are predicted to function as calcium transporters. The authors went on to demonstrate that components of the MTRC are localized on the cell surface but not in the cilia. They also presented findings that support the conclusion that the mating type-specific region of the MTA and MTB genes can influence both self- and non-self-recognition in mating.

      Taken together, the findings presented are interesting and extend our understanding of how organisms with more than two mating types/sexes may be specified. The identification of the six-protein MRC complex is quite intriguing. It would seem important that the function of at least one of these subunits be analyzed by gene deletion and phenotyping, similar to the findings presented here for the MTA and MTB mutants. A straightforward prediction might be that a deletion of any subunit of the MRC complex would result in a sterile phenotype. The manuscript was very well written and a pleasure to read.

      Thanks for the valuable comments and suggestions. We are currently in the process of constructing deletion strains for these genes. As of now, we have successfully obtained ΔMRC1-3 and MRC4-6 knockdown strains. Our preliminary observations indicate that ΔMRC1-3 strains are unable to undergo mating. However, we prefer not to include these results in the current manuscript, as we believe that more comprehensive studies are still needed.

      Reviewer #3:

      The authors describe the role, location, and function of the MTA and MTB mating type genes in the multi-mating-type species T. thermophila. The ciliate is an important group of organisms to study the evolution of mating types, as it is one of the few groups in which more than two mating types evolved independently. In the study, the authors use deletion strains of the species to show that both mating types genes located in each allele are required in both mating individuals for successful matings to occur. They show that the proteins are localized in the cell membrane, not the cilia, and that they interact in a complex (MTRC) with a set of 6 associated (non-mating type-allelic) genes. This complex is furthermore likely to interact with a cyclin-dependent kinase complex. It is intriguing that T. thermophila has two genes that are allelic and that are both required for successful mating. This coevolved double recognition has to my knowledge not been described for any other mating-type recognition system. I am not familiar with experimental research on ciliates, but as far as I can judge, the experiments appear well performed and mostly support the interpretation of the authors with appropriate controls and statistical analyses.

      The results show clearly that the mating type genes regulate non-self-recognition, however, I am not convinced that self-recognition occurs leading to the suppression of mating. An alternative explanation could be that the MTA and MTB proteins form a complex and that the two extracellular regions together interact with the MTA+MTB proteins from different mating types. This alternative hypothesis fits with the coevolution of MTA and MTB genes observed in the phylogenetic subgroups as described by Yan et al. (2021 iScience). Adding MTAxc and/or MTBxc to the cells can lead to the occupation of the external parts of the full proteins thereby inhibiting the formation of the complex, which in turn reduces non-self interactions. Self-recognition as explained in Figure 2S1 suggests an active response, which should be measurable in expression data for example. This is in my opinion not essential, but a claim of self-recognition through the MTA and MTB should not be made.

      We express our gratitude to Reviewer #3 for proposing the occupation model and have incorporated this possibility into the manuscript. We believe it is possible that occupation may serve as the molecular mechanism through which self-recognition negatively regulates mating. If there is a physical interaction between mating-type proteins of the same type, but this interaction blocks the recognition machinery rather than initiating mating, it can be considered a form of self-recognition. This aligns with the observation that strains expressing MTA/B6 and MTB2 mate normally with WT cells of all mating types except for VI and II (line 203-204). A concise discussion on this topic is included in the manuscript (line 288-293, 659-661). We are actively investigating the downstream aspects of mating-type recognition, and we hope to provide further insights into this question soon.

      The authors discuss that T. thermophila has special mating-type proteins that are large, while those of other groups are generally small (lines 157-160 and discussion). The complex formed is very large and in the discussion, they argue that this might be due to the "highly complex process, given that there are seven mating types in all". There is no argument given why large is more complex, if this is complex, and whether more mating types require more complexity. In basidiomycete fungi, many more mating types than 7 exist, and the homeodomain genes involved in mating types are relatively small but highly diverse (Luo et al. 1994 PMID: 7914671). The mating types associated with GPCR receptors in fungi are arguably larger, but again their function is not that complex, and mating-type specific variations appear to evolve easily (Fowler et al 2004 PMID: 14643262; Seike et al. 2015 PMID: 25831518). The large protein complex formed is reminiscent of the fusion patches that develop in budding or fission yeasts. In these species, the mating type receptors are activated by ligand pheromones from the opposite mating type that induce polarity patch formation (see Sieber et al. 2023 PMID: 35148940 for a recent review). At these patches, growth (shmooing) and fusion occur, which is reminiscent (in a different order) of the tip transformation in T. thermophilia. The fusion of two cells is in all taxa a dangerous and complex event that requires the evolution of very strict regulation and the existence of a system like the MTRC and cyclin-dependent complex to regulate this process is therefore not unexpected. The existence of multiple mating types should not greatly complicate the process, as most of the machinery (except for the MTA and MTB) is identical among all mating types.

      We are very grateful that Reviewer #3 provide this insightful view and relevant papers. In response to the feedback, we removed the sentences regarding “multiple mating types greatly complicate the process” in the revised version. Instead, we have introduced a discussion section comparing the mating systems of yeasts and Tetrahymena (line 279-286).

      The Tetrahymena/ciliate genetics and lifecycle could be better explained. For a general audience, the system is not easy to follow. For example, the ploidy of the somatic nucleus with regards to the mating type is not clear to me. The MAC is generally considered "polyploid", but how does this work for the mating type? I assume only a single copy of the mating type locus is available in the MAC to avoid self-recognition in the cells. Is it known how the diploid origin reduces to a single mating type? This does not become apparent from Cervantes et al. 2013.

      In T. thermophila, the MIC (diploid) contains several mating-type gene pairs (mtGP, i.e., MTA and MTB) organized in a tandem array at the mat locus on each chromosome. In sexual reproduction, the new MAC of the progeny develops from the fertilized MIC through a series of genome editing events, and its ploidy increases to ~90 by endoreduplication. During this process, mtGP loss occurs, resulting in only one mtGP remaining on the MAC chromosome. The mating-type specificity of mtGPs on each chromosome within one nucleus becomes relatively pure through intranuclear coordination. After multiple assortments (possibly caused by MAC amitosis during cell fission), only mtGPs of one mating-type specificity exist in each cell, determining the cell’s mating type.

      It is pity that the exact mechanisms involved in this complicated process remain a black box. The loss of mating-type gene pairs is hypothesized to involve a series of homologous recombination events, but this has not been completely proven. Furthermore, there is no clear understanding of how intranuclear coordination and assortment are achieved. While we have made observations confirming these events, a breakthrough in understanding the molecular mechanism is yet to be achieved.

      We included more information in the revised version (line 672-683). Given the complexity of these unusual processes, we recommend an excellent review by Prof. Eduardo Orias (PMID: 28715961), which offers detailed explanations of the process and related concepts (line 685-686).

      Also, the explanation of co-stimulation is not completely clear (lines 49-60). Initially, direct cell-cell contact is mentioned, but later it is mentioned that "all cells become fully stimulated", even when unequal ratios are used. Is physical contact necessary? Or is this due to the "secrete mating-essential factors" (line 601)? These details are essential, for interpretation of the results and need to be explained better.

      Sorry that we didn’t realize the term “contact” is not precise enough. In Tetrahymena, physical contact is indeed necessary, but it can refer to temporary interactions. Unlike yeast, Tetrahymena cells exhibit rapid movement, swimming randomly in the medium. Occasionally, two cells may come into contact, but they quickly separate instead of sticking together. Even newly formed loose pairs often become separated. As a result, one cell can come into contact with numerous others and stimulate them. We have clarified this aspect in the revised version (line 50-51, 57).

      Abstract and introduction: Sexes are not mating types. In general, mating types refer to systems in which there is no obvious asymmetry between the gametes, beyond the compatibility system. When there is a physiological difference such as size or motility, sexes are used. This distinction is of importance because in many species mating types and sexes can occur together, with each sex being able to have either (when two) or multiple mating types. An example are SI in angiosperms as used as an example by the authors or mating types in filamentous fungi. See Billiard et al. 2011 [PMID: 21489122] for a good explanation and argumentation for the importance of making this distinction.

      We have clarified the expression in the revised version (line 20, 38, 40, 45).

      Recommendations for the authors:

      Reviewer #1:

      I really enjoyed reading this manuscript and I think a few tweaks in the writing/data presentation could greatly improve the experience for the reader:

      (1) The information about your previous work in identifying downstream proteins CDK19, CYC9, and CIP1 (lines 170-173) could be directly presented in the introduction.

      We have moved this information in the introduction in the revised version (line 74-77).

      (2) For a reader who is not familiar with Tetrahymena, a few more details on how reporter and knock-out lines are generated would be beneficial.

      We introduced the knock-out method in Figure 2 – figure supplement 1B, HA-tag method in Figure 3A, and MTB2-eGFP construction method in Figure 4E. In addition, we introduced how co-stimulation markers observed in Materials and Methods (line 404-410)

      (3) Figures 5 and 6: clarify the types of pairing and treatments that were done directly in the figure (eg. adding additional labels). As of now, it is necessary to go through the text and legend to try and understand in detail what was done.

      Cell types and treatments were directly introduced in the revised figure (Figure 5 and 6).

      (4) The logical transition in lines 136-142 is hard to follow.

      We rewrote this paragraph in the revised version (lines 143-156). Additionally, we added a figure to illustrate the theoretical mating-type recognition model between WT cells and ΔCDK19, ΔCYC9 cells, MTAxc, MTBxc proteins, and ΔMTA, ΔMTB cells (Figure 2 – figure supplement 1D-G).

      (5) Lines 191-196: the fact that cells expressing multiple mating types can self goes against an active self-rejection system - if this is the case there should be self-rejection among all expressed mating types. Unless non-self recognition is an active process and self-recognition is simply the absence of non-self recognition. The authors briefly mention this in lines 263-265, but it would be interesting to expand and clarify this.

      We appreciate that Reviewer #1 notice the interesting selfing phenotype of the MTB2-eGFP (MTVI background) strain. We further discussed it in the revised manuscript (line 298-306).

      (6) The authors briefly mention the possibility of different mating types using different recognition mechanisms (lines 255-260), based on the big differences in the size of the mating-specific region of MT proteins. Following this and the weakness nr. 2, I think it would be pertinent to gather and present more information on the properties and structures of the mating-type specific regions of MT proteins. Simple in silico analysis of motifs, structure, etc. could help clarify the role of these regions. It seems more parsimonious that MT proteins would have variable mating type specific regions that account for the recognition of the different mating types, and conserved cytoplasmic functions that could trigger a single downstream signaling cascade. It would be interesting to know the authors' opinion on this.

      We are very grateful for this suggestion. Actually, we are currently working on determining the 3D structure of MTRC. The Alphafold2 prediction indicates that the MT-specific region is comprised of seven global β-sheets, resembling the structure of immunoglobulins (Ig). Our most recent cryo-EM results have revealed a ~15Å structure, aligning well with the prediction. However, the main challenge lies in the low expression levels, both in Tetrahymena and insect/mammal cells. We anticipate obtaining more detailed results soon. Therefore, we prefer to present the MT recognition model with robust experimental evidence in the future, and didn’t discuss too much on this aspect in the current manuscript.

      (7) Adding a figure including a proposed model, as well as expanding the discussion on the points presented as "weaknesses" would help clarify the ideas/hypothesis on how the mating recognition works. I think this would really elevate the paper and help highlight the results.

      We added a figure to introduce the model and the weaknesses in the revised version (Figure 7, line 656-665).

      (8) Line 202-203: It is far-fetched to infer subcellular localization based on the data presented here, couterstaining with other dyes and antibodies specific to certain cell components, as well as negative control images, are required.

      Thanks for the suggestion. We attempted to stain cell components using various dyes and antibodies. Unfortunately, we found that cell surface and cilia (especially oral cilia) is very easy to give a false positive signal. We think this issue seriously affects the credibility of the results. It may seem like splitting hairs, but we are trying to be precise.

      Meanwhile, we still believe the mating-type proteins localizes to cell surface because MTA-HA is identified in the isolated cell surface proteins.

      Regarding negative control, as shown in Fig. 4G, where a MTB2-eGFP cell is pairing with a WT cell, no GFP signal is observed in the WT cell.

      (9) Lines 131: clarify the sentence - expression of Con-A receptors requires both MTA and MTB (MTA to receive the signal).

      We modified the sentence in the revised version (line 139-140).

      Reviewer #2:

      Minor points.

      (1) Line 194-196. Why are these cells able to self?

      These cells able to self may because the MTRC contain heterotypic mating-type proteins (MTA6 and MTB2), which activate mating when they interact with another heterotypic MTRC (line 207-208).

      (2) Line 232. What do the authors mean by the term synergistic effect here? Definition and statistics?

      Sorry about the confusion. The synergistic effect refers to the effect of MTAxc and MTBxc become stronger when using together. We clarified it in the revised version (line 232).

      (3) For Figure 4 panel D, are there antibodies that are available as a control for cilia? If so, then blotting this membrane would show that cilia-associated proteins are in the cilia preparation, which is a standard control for sub-cellular fractionation.

      Thanks for the suggestion. Unfortunately, we didn’t find a suitable cilia-specific antibody yet. Instead, we employed MS analysis to confirm the presence of cilia proteins in this sample (line 195-196, Figure 4–Source data 1). We also observed the sample under the microscope, which directly revealed the presence of cilia (Figure 4C).

      (4) At least one reference cited in the text was not present in the reference list. The authors should go through the references cited to ensure that all have made it into the reference list.

      We have checked all the references.

      Some minor edits:

      (1) MTA and MTB are presented in both roman and italics (e.g. line 209) in the manuscript. Maybe all should be in italics? Or is this a distinction between the gene and the protein?

      The italics word (MTA) refers to gene, and non-italics word (MTA) refers to protein.

      (2) Line 251. Change "achieving" to "achieve".

      We have corrected this word (line 266).

      Reviewer #3:

      Line 101. It would help to explain this expectation earlier in this paragraph.

      We explained the expectation in the revised version (line 92-97, 104-106).

      Line 109. How is a co-receptor different from the MTRC complex?

      We have rewritten the relevant sentences to enhance clarity (line 116-119). The molecular function of the MTRC complex could involve acting as a co-receptor or recognizer (functioning as both ligand and receptor). Based on the results presented in this section, we propose that MTA and MTB may function as a complex, but the confirmation of this hypothesis (MTRC) is provided in a later section. Therefore, we did not use the term “MTRC” here. These sentences briefly discuss the molecular function of this complex and explain why MTRC does not appear to function as a co-receptor.

      Line 251: which "dual approach" is referred to?

      Dual approach is referred to both self and non-self recognition. We explained it in the revised version (line 265-266).

      Line 258: what "different mechanisms" do the authors have in mind? Why would a different mechanism be expected? The different sizes could have evolved for (coevolutionary?) selection on the same mechanism.

      Sorry about the confusion. We clarified it in the revised version (line 269-278).

      What we intended to express is that we are uncertain whether the mating-type recognition model we discovered in T. thermophila is applicable to all Tetrahymena species due to significant differences in the length of the mating-type-specific region. We believe it is important to highlight this distinction to avoid potential misinterpretations in future studies involving other Tetrahymena species. At the same time, we look forward to future research that may provide insights into this question.

      Fig 2 C&D. Is it correct that these figures show the strains only after 'preincubation'? This is not apparent from the caption of the text. Additionally, the order of the images is very confusing. Write in the figures (so not just in the caption) what the sub-script means.

      These panels are re-organized in the revised version (Fig. 2C&D). There are three kinds of pictures: “not incubated”, “WT pre-incubated by mutant” and “mutant pre-incubated by WT”.

      The methods used to generate Figure 5 are not clearly described. I understand that the obtained xc proteins were added to the cells, and then washed, after which a test was performed mixing WT-VI and WT-VII cells. Were both cells treated? Or only one of the strains? The explanation for the reused washing medium is not clear and the method is not indicated.

      Both cells are treated. More details are provided in the revised manuscript (line 230-231, 633-634, 637-639, Fig. 5). To prepare the starvation medium containing mating-essential factors, cells were starved in fresh starvation medium for ~16 hours. Subsequently, cells were removed by three rounds of centrifugation (1000 g, 3 min) (line 330-332).

      In general, the figures are difficult to understand without repeated inquiries in the captions. Give more information in the figures themselves.

      More information is introduced in the figure (Fig. 2C, Fig. 3B, Fig. 4A, B, D, Fig. 5 and Fig. 6).

  3. Jul 2023
    1. Author Response

      The following is the authors’ response to the original reviews.

      Reviewer #1 (Public Review):

      This study presents an important finding on human m6A methyltransferase complex (including METTL3, METTL14 and WTAP). The evidence supporting the claims of the authors is convincing, although the model and assays need to be further modified. The work will be of interest to biologists working on RNA epigenetics and cancer biology.

      In mammals, a large methyltransferase complex (including METTL3, METTL14 and WTAP) deposits m6A across the transcriptome, and METTL3 serves as its catalytic core component. In this manuscript, the authors identified two cleaved forms of METTL3 and described the function of METTL3a (residues 239-580) in breast tumorigenesis. METTL3a mediates the assembly of METTL3-METTL14-WTAP complex, the global m6A deposition and breast cancer progression. Furthermore, the METTL3a-mTOR axis was uncovered to mediate the METTL3 cleavage, providing potential therapeutic target for breast cancer. This study is properly performed and the findings are very interesting; however, some problems with the model and assays need to be modified. It is widely known that METTL3 and METTL14 form a stable heterodimer with the stoichiometric ratio of 1:1 (Wang X et al. Nature 534, 575-578 (2016), Su S et al. Cell Res 32(11), 982994 (2022), Yan X et al. Cell Res 32(12), 1124-1127 (2022)), the numbers of METTL3 and METTL14 in the model of Fig 7P are not equivalent and need to be modified.

      We thank for reviewer’s good suggestion. We have modified the model in Fig. 7P.

      Reviewer #2 (Public Review):

      In this study, Yan et al. report that a cleaved form of METTL3 (termed METTL3a) plays an essential role in regulating the assembly of the METTL3-METTL14-WTAP complex. Depletion of METTL3a leads to reduced m6A level on TMEM127, an mTOR repressor, and subsequently decreased breast cancer cell proliferation. Mechanistically, METTL3a is generated via 26S proteasome in an mTOR-dependent manner.

      The manuscript follows a smooth, logical flow from one result to the next, and most of the results are clearly presented. Specifically, the molecular interaction assays are welldesigned. If true, this model represents a significant addition to the current understanding of m6A-methyltransferase complex formation.

      A few minor issues detailed below should be addressed to make the paper even more robust. The specific comments are contained below.

      1) The existence of METTL3a and METTL3b.<br /> In this study, the author found the cleaved form of METTL3 in breast cancer patient tissues and breast cancer cell lines. Is it a specific event that only occurs in breast cancer? The author may examine the METTL3a in other cell lines if it is a common rule.

      We thank reviewer for point this out. We discovered the cleaved form of METTL3 in breast cancer, and we further examined this cleaved METTL3 in other cell lines such as lung cancer cell lines, renal cancer cell lines, HCT116 and MEF (new Supplementary Figures 1A-1C), these data suggest that it is a common rule. Therefore, we speculate that METTL3a may be ubiquitiously expressed. We have added this part in the revised manuscript, please see Line 118-120.

      2) Generation of METTL3a and METTL3b.

      1) Figure 1 shows that METTL3a and METTL3b were generated from the C-terminal of full-length METTL3. Because the sequence of METTL3a is involved in the sequences of METTL3b, can METTL3b be further cleaved to produce METTL3a?

      Although the sequence of METTL3a is involved in the sequences of METTL3b, overexpression of METTL3b in T47D, MDA-MB-231 and 293T cells did not show METTL3a expression in these cells (please see Figures 3A, 3C, 3G), suggesting that METTL3b can not be further cleaved to produce METTL3a, and the METTL3 cleavage may require its N-terminal region. We have added this in the discussion, please see Line 358 to 360.

      2) Based on current data, the generation of METTL3a and METTL3b are separated. Are there any factors that affect the cleavage ratio between METTL3a and METTL3b?

      We thank for reviewer’s excellent question. In this study, we show that both METTL3a and METTLb are produced through proteasomal cleavage, and both of them are positively regulated by the mTOR pathway. On the other hand, we indeed observed the differential cleavage ratios between METTL3a and METTL3b across different cell lines. For example, METTL3a/METTLb ratio was greater than 1 in MDA-MB-231 cells (see Figure 7C), less than 1 in T47D and 293T cell lines (see Figure 7A and 7B), and equal to 1 in MEF cells (see Figure 7O). Based on these results, we speculate that there may be some factors that control the cleavage ratio between METTL3a and METTL3b, which warrants further investigation. We have added this in the discussion, please see Line 374 to 379.

      3) In Figure 2G, the author shows the result that incubation of the Δ198+Δ238 METTL3 protein with T47D cell lysates cannot produce the METTL3a and METTL3b variants. The author may also show the results that Δ198 METTL3 protein or Δ238 METTL3 protein incubates with T47D cell lysates, respectively.

      Following the reviewer’s suggestion, we had performed in vitro cleavage assays by incubation of METTL3-Δ238 or METTL3-Δ198 with T47D cell lysates, and had incorporated this result in the revised manuscript. Please see our new Supplementary Figure 3A.

      4) As well as many results published in previous studies, the in vitro methylation assay shows that WT METTL3 is capable of methylating RNA probe (figure 2H). The main point of this study is that METTL3a is required for the METTL3-METTL14 assembly. However, the absence of METTL3a in the in vitro system did not inhibit METTL3METTL14 methylation activity. Moreover, the presence of METTL3a even resulted in a weak m6A level.

      The main point of this study is that METTL3a is required for the METTL3WTAP interaction, but dispensable for the METTL3-METTL14 assembly (see Figure 4A-4B). In this in vitro methylation assays, METTL3 and METTL14 is capable of methylating RNA probe in the absent of WTAP. In this condition, we found that METTL3 WT as well as its different variants (METTL3-Δ238, METTL3-Δ198, METTL3b and METTL3a) except the catalytically dead mutant METTL3 APPA showed methylation activity in vitro.

      5) In Figure 4A, the author suggests that WTAP cannot be immunoprecipitated with METTL3a and 3b because WTAP interacted with the N-terminal of METTL3. If this assay is performed in WT cells, the endogenous full-length METTL3 may help to form the complex. In this case, WTAP is supposed to be co-immunoprecipitated.

      We thank reviewer for point this out. METTL3 interacts with WTAP through its N-terminal (1-33aa) (1). Consistently, we find that the two cleaved forms METTL3a and METTL3b which lack the N-terminal region are not able to bind with WTAP. In Figure 4A, we overexpressed METTL3 WT as well as its different variants METTL3-Δ238, METTL3-Δ198, METTL3b and METTL3a respectively in WT cells, and compared the binding ability with WTAP or METTL14 across these overexpressed METTL3 variants. We acknowledge that the exogenous METTL3a and METTL3b interact with endogenous full-length METTL3, and the endogenous full-length METTL3 may help them to form the complex with WTAP. But in fact, the exogenous expression levels of METTL3a and METTL3b are much higher than that of endogenous full-length METTL3 (see Figure 3A and 3C). In this case, METTL3a or METTL3b predominantly interacts with itself, METTL3, METTL14 or other potential interacting proteins through its C-terminal region, this may greatly dilute the condition for the interaction between WTAP and endogenous full-length METTL3. Moreover, in Figure 4A, the comparison is among overexpressed METTL3 variants, the week indirect interactions through much lower expression levels of endogenous protein are probably not comparable to those direct interactions between overexpressed METTL3 variants and WTAP.

      Reference:

      1) Schöller, E., Weichmann, F., Treiber, T., Ringle, S., Treiber, N., Flatley, A., Feederle, R., Bruckmann, A., and Meister, G. (2018). Interactions, localization, and phosphorylation of the m6A generating METTL3–METTL14–WTAP complex. Rna 24, 499-512

      Reviewer #1 (Recommendations For The Authors):

      Major points:

      1) It is widely known that METTL3 and METTL14 form a stable heterodimer with the stoichiometric ratio of 1:1 (Wang X et al. Nature 534, 575-578 (2016), Su S et al. Cell Res 32(11), 982-994 (2022), Yan X et al. Cell Res 32(12), 1124-1127 (2022)), the numbers of METTL3 and METTL14 in the model of Fig 7P are not equivalent and need to be modified.

      We thank for reviewer’s good suggestion. We have modified the model in Fig. 7P.

      2) The in vitro methylation activity was detected by the m6A antibody, which has limited linear range. The MTase-Glo{trade mark, serif} Methyltransferase Assay is a SAMdependent enzyme assay with wide applications (Please refer to the references below).

      Could this assay be performed by authors?

      Wilkinson AW et al. Nature 565(7739), 372-376 (2019).

      Yu D et al. Nucleic Acids Res 49(20),11629-11642 (2021).

      Yan X et al. Cell Res 32(12), 1124-1127 (2022).

      Chen J et al. Nat Commun 13(1), 3257 (2022).

      Thanks for reviewer’s good suggestion. We had performed the in vitro methylation assay by using MTase-Glo kit, and the data is consistent with the dot blot results. Please see the new Figure 2H-J.

      3) When expressed alone in mammalian cell lines, METTL14 is unstable and is easily contaminated with endogenous METTL3 during purification (Yang W et al. Nat Cell Biol 16(2), p.191-8 (2014), Fig 1e). In Fig 2I, Co-expressing METTL3 and METTL14 maybe a good choice.

      We thank for reviewer’s good suggestion. In fact, we co-expressed METTL3 and METTL14 in this in vitro methylation assay in Fig 2I (new Figure 2J in the revised version), METTL3-Flag or its mutant with Flag tag and METTL14-Flag were co-transfected into 293T cells, and co-purified by using Flag M2 magnetic beads from the cell lysates. We have added these details in the indicated method section, please see Line 574-585.

      Other minor points:

      1) In Fig 5D, the protein domain information of METTL3 and relevant references need to be added (Su S et al. Cell Res 32(11), 982-994 (2022), Fig 6g; Yan X et al. Cell Res 32(12), 1124-1127 (2022), Fig 1a).

      We have added these references in the revised manuscript.

      2) In Fig 5, would METTL3b contribute to the METTL3-METTL3 interaction?

      Our data showed that METTL3a but not METTL3b is responsible for the METTL3-WTAP interaction, breast cancer cell proliferation and the m6A modification. Then, we investigated the mechanism of how METTL3a regulates the METTL3-WTAP interaction, and found that METTL3a is essential for METTL3-METTL3 interaction, which is a prerequisite step for WTAP recruitment in MTC complex. In this case, we speculate that METTL3b is not required for the METTL3-METTL3 interaction. Indeed, through Co-IP assays,we found that METTL3b has no effect on the METTL3-METTL3 interaction (new supplementary Figure 4D), which is consistent with our above data showing that METTL3b is dispensable for the METTL3-WTAP interaction. We have added this comment in Page 6, Line 226 to 228.

      3) In Fig 3F, the color in the legend and figure is inconsistent.

      We have corrected the inconsistent color in the revised manuscript.

      Reviewer #2 (Recommendations For The Authors):

      1) In Figure 5D, the construction details of METTL3-HA and Flag should have been included in the method section. Are these tag sequences in the N-terminal of METTL3 protein?

      These tags are all in the C-terminal of METTL3. We have added the construction details of these plasmids in the method section. Please see Line 434.

      2) In Figure 7A, the labels of the inhibitors are overlapped with the figures.

      We have corrected the labels of the inhibitors in Figure 7A in the revised manuscript.

  4. Feb 2023
    1. Author Response

      Reviewer #1 (Public Review):

      In this work, the authors investigate a means of cell communication through physical connections they call membrane tubules (similar or identical to the previously reported nanotubes, which they reference extensively). They show that Cas9 transfer between cells is facilitated by these structures rather than exosomes. A novel contribution is that this transfer is dependent on the pair of particular cell types and that the protein syncytin is required to establish a complete syncytial connection, which they show are open ended using electron microscopy.

      The data is convincing because of the multiple readouts for transfer and the ultrastructural verification of the connection. The results support their conclusions. The implications are obvious, since it represents an avenue of cellular communication and modifications. It would be exciting if they could show this occurring in vivo, such as in tissue. The implication of this would be that neighboring cells in a tissue could be entrained over time through transfer of material.

      Thank the reviewer for his/her comments and suggestion. It’s possible that the thick tubular connections found in this study also exist in vivo. A previous study reported that TNT-like structures were found in mouse or human primary tumor cells (PMID: 34494703; PMID: 34795441). Our transfer assays could be adopted to evaluate such transfer in primary cultures and in vivo. We anticipate this for future work.

      Reviewer #2 (Public Review):

      There is a lot of interest in how cells transfer materials (proteins, RNA, organelles) by extracellular vesicles (EV) and tunneling nanotubes (TNTs). Here, Zhang and Schekman developed quantitative assays, based on two different reporters, to measure EV and direct contact-dependent mediated transfer. The first assay is based on transfer of Cas9, which then edits a luciferase gene, whose enzymatic activity is then measured. The second assay is based on a split-GFP system. The experiments on EV trafficking convincingly show that purified exosomes, or any other diffusible agent, are unable to transfer functional Cas9 (either EV-tethered or untethered) and induce significant luciferase activity in acceptor cells. The authors suggest a plausible model by which Cas9 (with the gRNA?) gets "stuck" in such vesicles and is thus unable to enter the nucleus to edit the gene.

      To test alternative pathways of transfer, e.g. by direct cell-cell contact, the authors co-cultured donor and acceptor cells and detect significant luciferase activity. The split GFP assay also showed successful transfer. The authors further characterize this process by biochemical, genetic and imaging approaches. They conclude that a small percentage of cells in the population produce open-ended membrane tubules (which are wider and distinct from TNTs) that can transfer material between cells. This process depends on actin polymerization but not endocytosis or trogocytosis. The process also seems to depend on endogenously expressed Syncytin proteins - fusogens which could be responsible for the membrane fusion leading to the open ends of the tubules.

      The paper provides additional solid evidence to what is already known about the inefficiency of EV-mediated protein transport. Importantly, it provides an interesting new mechanism for contact-dependent transport of cellular material and assigns valuable new information about the possible function of Syncytins. However, the evidence that the proteins and vesicles transfer through the tubules is incomplete and a few more experiments are required. In addition, certain inconsistencies within the paper and with previous literature need to be resolved. Finally, some parts of the text, methods and the figures require re-writing or additional information for clarity.

      Major comments

      1) In Figure 1F, the authors compare the function of exosome-transported SBP-Cas9-GFP vs. transient transfection of SBP-Cas9-GFP. It is not clear if the cells in the transiently transfected culture also express the myc-str-CD63 and were treated with biotin. It is important to determine if CD63-tethering itself affects Cas9 function.

      Thank the reviewer for his comments and suggestions. We now show in Figure 1- figure supplement 1D that CD63-tethering itself does not affect Cas9 function.

      2) The authors do not rule out that TNTs are a mode of transfer in any of their experiments. Their actin polymerization inhibition experiments are also in-line with a TNT role in transfer. This possibility is not discussed in the discussion section.

      Yes, the results in this study do not rule out a role for TNTs in the transfer. At present, we are not aware of conditions that would functionally distinguish transfer mediated by TNTs and thick tubules. We have now included this in the Discussion section.

      3) Issues with the Split GFP assay:

      a) On page 4, line 176, the authors claim that "A mixture of cells before co-culture should not exhibit a GFP signal". However, this result is not presented.

      The results of mixture experiment are included in Figure 2-figure supplement 1D, E.

      b) The authors show in Figure 2C and F that in MBA/HEK co-culture or only HEK293T co-culture, there are dual-labeled, CFP-mCherry, cells. First - what is the % of this sub-population? Second, the authors dismiss this population as cell adhesion (Page 5, line 192) - but in the methods section they claim they gated for single particles (page 17, line 642), supposedly excluding such events. There is a simple way to resolve this - sort these dual labeled cells and visualize under the microscope. Finally - why do the authors think that the GFP halves can transfer but not the mature CFP or mCherry?

      The plot in the Figure 2C and F are displayed in an all-cell mode, not in singlet mode. The percentage of dual-labeled CFP-mCherry in singlet was 0-0.2%. Thus, most of the signal was from doublet, or cell adhesion. We did not claim that the mature CFP or mCherry cannot be transferred. We suggested that the GFP signal of split-GFP recombination may be a more accurate reflection of cytoplasmic transfer between cells. In contrast, mature CFP or mCherry may simply attach to the cell surface but not enter into the other cells.

      c) In the Cas9 experiments - the authors detect an increase in Nluc activity similar in order of magnitude that that of transient transfection with the Cas9 plasmid - suggesting most acceptor cells now express Nluc. However, only 6% of the cells are GFP positive in the split-GFP assay. Can the authors explain why the rate is so low in the split-GFP assay? One possibility (related to item #2 above) is that the split-GFP is transferred by TNTs.

      The Cas9-based Nluc activity assay is more sensitive as it measures an enzyme with a very high turnover number. The split-GFP assay requires a transfer of GFP fragments to produce intact GFP molecules where the signal is not amplified. We think this explains the dramatic increase in a signal once Cas9 is transferred. Our cell sorting results suggest that at least 6% of the receptor cells are transferred in the co-cultures. Of course, nothing in either analysis rules out a role for TNTs in this transfer.

      4) The membrane tubules, the membrane fusion and the transfer process are not well characterized:

      a) The suggested tubules are distinct from TNTs by diameter and (I presume, based on the images) that they are still attached to the surface - whereas TNTs are detached. However, how are these structures different from filopodia except that they (rarely) fuse?

      We used TIRF microscopy and found that the thick tubules are not attached to the surface (not shown). Filopodia are much closer in diameter to TNTs (0.1-0.4 micron). The thick tubules we observe are much thicker (2-4 micron in diameter).

      b) Figure 5E shows that the acceptor cells send out a tubule of its own to meet and fuse. Is this the case in all 8 open-ended tubules that were imaged? Is this structure absent in the closed-ended tubules (e.g. as seen in Figures 6 & 8)?

      Around half of open-ended tubules appeared to emanate from acceptor cells. Likewise, for closed-ended tubules, for example, in Figure 6E where a recipient HEK293T cell projected a short tubule.

      c) The authors suggest a model for transport of the proteins tethered to vesicles (via CD63 tethering). However, the data is incomplete.

      i) They show only a single example of this type of transport, without quantification. How frequent is this event?

      The transport of the proteins tethered to vesicles (via CD63 tethering) were found in all 8 open-ended tubules that we detected in this study.

      ii) Furthermore, the labeling does not conclusively show that these are vesicles and not protein aggregates. Labeling of the vesicle - by dye or protein marker will be useful to determine if these are indeed vesicles, and which type.

      In Figure 4B, the moving punctum in a tubular connection appears to contain SBP-Cas9-GFP, Streptavidin-CD63-mCherry, and the cell surface WGA conjugate that may have been internalized into a donor cell endosome, which indicates that the moving punctum is vesicle type. Nonetheless, in general we cannot distinguish the forms of Cas9 that are transferred and become localized to the nucleus of target cells and we make no claim other than to suggest this possibility that Cas9 may be transferred as an aggregate.

      iii) The data from Figure 2 suggest (if I understand correctly) transfer of the CD63-tethered half-GFP, further strengthening the idea of vesicular transfer. However, the authors also show efficient transfer of untethered Cas9 protein (Figure 2A and other figures). Does this mean that free protein can diffuse through these tubules? The Cas9 has an NLS so the un-tethered versions should be concentrated in the nucleus of donor cells. How, then, do they transfer? The authors do not provide visual evidence for this and I think it is important they would.

      Based on the results using the Cas9-based luciferase assay (His- or SBP-tagged Cas9) (Figure 2A) and split-GFP assay (free GFP1-10) (Figure 2G), we suggest that free protein could be transferred between cells. Our current imaging approach is not designed to quantify protein diffusion. However, we are able to detect from images that Cas9-GFP does not colocalize exclusively with CD63 or concentrate in the nucleus, but also appears in the cytoplasm. These data indicate that both vesicle association and free diffusion may mediate the transfer through tubules. We thank the referee for emphasizing this issue which we will consider for future work to distinguish the transfer types through tubules.

      iv) In Figures 6 & 8, where transfer is diminished, there are still red granules in acceptors cells (representing CD63-mcherry). Does this mean that vesicles do transfer, just not those with Cas9-GFP? Is this background of the imaging? The latter case would suggest that the red granule moving from donor to acceptor cells in figure 4 could also be "background". This matter needs to be resolved.

      There are a few red puncta in the acceptor cell in Figure 6B. Since the acceptor cell is close to and overlapped with other donor cells containing CD63-mCherry, the red signal may, as the reviewer suggests, be from donor cells and not as a result of transfer through tubular connections. However, donor-acceptor cultures of HEK293T where transfer is not observed, little CD63-mCherry signal, for example, in Figure 6a, was seen in acceptor cells, even during several hours of observation (Figure 6- figure supplement video). A minor red signal could arise from exosomes secreted by donor cells that are internalized by acceptor cells. Images of single-culture receptor cells were added in Figure 4- figure supplement 1.

      For Figure 8, we used MDA-MB-231 syncytin-2 knock-down cells containing Fluc:Nluc:mCherry as the receptor cell, thus in these experiments the red signal most likely represents mCherry expressed in the acceptor cells.

      In Figure 4, we observed moving punctum in a tubular connection which contained co-localized green, red, and purple signals, corresponding to SBP-Cas9-GFP, streptavidin-CD63-mCherry, and the WGA conjugate, respectively. The video of punctum transport (Figure 4-figure supplement video) suggests that the red signal is not “background”.

      5) Why do HEK293T do not transfer to HEK293T?

      a) A major inexplicable result is that HEK293T express high levels of both Syncytin proteins (Figure 7 - supp figure 1A) yet ectopic expression of mouse Syncytin increases transfer (Figure 7E). Why would that be? In addition, Fig 3A shows high transfer rates to A549 cells - which express the least amount of Syncytin. The authors suggest in the discussion that Syncytin in HEK293T might not be functional without real evidence.

      We cannot yet explain why the basal level of syncytin expressed in HEK293 cells is insufficient to promote open-ended tubular connections between these cells. It could be that the proteins are not well represented in a processed form at the cell surface. Nonetheless, ectopic expression of mouse syncytin-A in HEK293T produced some increased transfer but less than when syncytin-A is ectopically expressed in MDA-MB-231 cells (up to 4-fold vs. 30-fold change of Nluc/Fluc signal) (Figure 7E). Furthermore, we have added new results which show that apparent furin-processed forms of syncytin-A, -1 and -2 can be detected by cell surface biotinylation in transfected MDA-MB-231 cells (Figure 8-figure supplement 1D). All we demonstrate is that syncytin in the acceptor cell is required for fusion and we make no claim that it is the only protein or lipid at the cell surface in the acceptor cell required for fusion. Clearly, more work is essential to establish the complexity of this fusion reaction.

      For A549 cells, syncytin-1 is highly expressed in A549 cells, thus it is possible that syncytin-1 in A549 plays crucial roles in the process.

      b) In addition - previous publications (e.g. PMID: 35596004; 31735710) show that over expression of syncytin-1 or -2 in HEK293T cells causes massive cell-cell fusion. The authors do not provide images of the cells, to rule out cell-cell fusion in this particular case.

      Overexpression of syncytin-1 or -2 in cells indeed causes massive cell-cell fusion, while overexpression of syncytin-A induced much less cell fusion than syncytin-1, or -2. We have now added new images shown in Figure 8-figure supplement 1A-C to document these observations. It may be that overexpressed human syncytins are better represented in a furin-processed form in both cell types. In contrast, we did not observe donor-acceptor cell fusion at basal levels of expression of syncytin in HEK293T and MDA-MB-231. For example, the Figure 4-figure supplement video shows that tubular structures were seen to form and break during the course of visualization with a tubule fusion event but no cell fusion to form heterokaryons.

      Reviewer #3 (Public Review):

      In this manuscript, Zhang and Schekman investigated the mechanisms underlying intercellular cargo transfer. It has been proposed that cargo transfer between cells could be mediated by exosomes, tunneling nanotubes or thicker tubules. To determine which process is efficient in delivering cargos, the authors developed two quantitative approaches to study cargo transfer between cells. Their reporter assays showed clearly that the transfer of Cas9/gRNA is mediated by cell-cell contact, but not by exosome internalization and fusion. They showed that actin polymerization is required for the intercellular transfer of Cas9/gRNA, the latter of which is observed in the projected membrane tubule connections. The authors visualized the fine structure of the tubular connections by electron microscopy and observed organelles and vesicles in the open-ended tubular structure. The formation of the open-ended tubule connections depends on a plasma membrane fusion process. Moreover, they found that the endogenous trophoblast fusogens, syncytins, are required for the formation of open-ended tubular connections, and that syncytin depletion significantly reduced cargo Cas9 protein transfer.

      Overall, this is a very nice study providing much clarity on the modes of intercellular cargo transfer. Using two quantitative approaches, the authors demonstrated convincingly that exosomes do not mediate efficient transfer via endocytosis, but that the open-ended membrane tubular connections are required for efficient cargo transfer. Furthermore, the authors pinpointed syncytins as the plasma membrane fusogenic proteins involved in this process. Experiments were well designed and conducted, and the conclusions are mostly supported by the data. My specific comments are as follows.

      1) The authors showed that knocking down actin (which isoform?) in both donor and acceptor cells blocked transfer, and more so in the acceptor cells perhaps due to the greater knockdown efficiency in these cells. However, Arp2/3 complex knockdown in donor cells, but not recipient cell, reduced Cas9 transfer. It would be good to clarify whether the latter result suggests that the recipient cells use other actin nucleators rather than Arp2/3 to promote actin polymerization in the cargo transfer process. Are formins involved in the formation of these tubular connections?

      We thank the reviewer for his/her comments and suggestions. Beta-actin was knocked down in this study. We tried a formin inhibitor, SMIFH2 which resulted in a decrease the Cas9 transfer between cells (Figure 3F).

      2) The authors provided convincing evidence to show that the tubular connections are involved in cargo transfer. Intriguingly, in Figure 4-figure supplement video (upper right), protein transfer appeared to occur along a broad cell-cell contact region instead of a single tubular connection. How often does the former scenario occur? Is it possible that transfer can happen as long as cells are contacting each other and making protrusions that can fuse with the target cell?

      In the Figure 4-figure supplement video (upper right), it may be that several membrane tubes from several different donor cells contact at sites close to one another on the recipient cell resulting in the appearance a broad cell-cell contact. This was a rare observation. In our quantification, only 8 connections were open-ended in 120 cell-cell contact junctions. Once open-ended, or plasma membrane fused, cargo transfer is observed.

      3) The requirement of MFSD2A in both donor (HEK293T) and recipient (MDA-MB-231) cells is consistent with a role for syncytin-1 or 2 in both types of cells. Since HEK293T cells contain both syncytins and MFSD2A but cargo transfer does not occur among these cells, does this suggest that syncytins and/or MFSD2A are only trafficked to the HEK293T cell membrane in the presence of MDA-MB-231 cells?

      A proper answer to this question requires the visualization of syncytins and MFSD2A. The commercial syncytin antibodies were inadequate for immunofluorescence. In advance of the more detailed effort required to tag the genes for endogenous syncytin 1 and 2, we performed live cell imaging and surface biotin labeling of cells transiently transfected to express fluorescently-tagged forms of syncytin-1, -2 and -A. We now show that syncytin-A, -1, and -2 partially localize to the plasma membrane or the cell surface of MDA-MB-231 and at points of cell-cell contact. In fact, overexpression of codon-optimized human syncytin-1, and -2 induced dramatic HEK293T cell-cell fusion. However, at basal levels of syncytin expression, HEK293T could not form open-ended tubular connections, which may be because the basal level of syncytins are not well represented in a processed form at the cell surface or their activity is limited by unknown factors.

      As an independent test of cell surface localization, we used surface biotinylation to show that a fraction of the syncytins can be labeled externally (Figure 8-figure supplement 1D). This fraction shows evidence of proteolytic processing consistent with furin cleavage whereas the overwhelming majority of transfected syncytins detected in a blot of lysates suggests that most remain in the unprocessed precursor form, consistent with the punctate and reticular fluorescence images (Figure 8-figure supplement 1A-C).

      We used IF and GFP-tagged MFSD2A and found this protein partially localized to the plasma membrane of HEK293T cells (Figure 9E, F). Given the results reveal that cargos could be transferred among MDA-MB-231 cells (Figure 2G), syncytin and its receptor appear to function in transfer among these cells.

  5. Dec 2022
  6. Aug 2022
    1. Note: This rebuttal was posted by the corresponding author to Review Commons. Content has not been altered except for formatting.

      Learn more at Review Commons


      Reply to the reviewers

      Reply to the reviewers

      1. General Statements

      It is the common view of all three reviewers that we have not utilized adequate in vitro/biochemical evidence to support the idea that SATB1 protein undergoes liquid-liquid phase separation. We do agree with the reviewers that our manuscript lacks biochemical evidence to support such notion. Though we find it quite interesting and we would like to suggest for the first time in the field of chromatin organization and function, based upon the action of SATB1, that this protein does exist in at least two polypeptide isoforms (764 and 795 amino acids long) which display different phase separation propensity and therefore confer different actions in regulating the (patho)physiological properties of a murine T cell.

      Every single research group that works on SATB1, considered so far only a single protein isoform, that is, the shorter isoform of 764 amino acids and no tools, such as isoform-specific antibodies have been developed to discriminate the two isoforms and thus being able to assign unique functions to each isoform. We do understand that such a report, suggesting the presence of two protein isoforms, with potentially quite diverse functions, would question (not necessarily by the authors of this manuscript, since no such comment is included in our manuscript) the conclusions drawn in the literature assigning all biochemical properties to a single, short isoform of SATB1. Moreover, all the genetically modified mice that have been analyzed so far (including our group), deleted both Satb1 isoforms. Our future research approaches should, from now on, consider unraveling the isoform-specific functions of SATB1 and their involvement in physiology and disease. This could also deem useful to explain the quite diverse, both positive and negative effects of SATB1 in transcription regulation. Another major objection of the reviewers was that we should provide cumulative supporting evidence for the existence of the long SATB1 isoform, or at least evaluate the specificity of our custom-made antibody.

      Taking under consideration the aforementioned constructive criticism of the three reviewers we would like to perform (most of the suggested experiments have already been performed) additional experiments to support our claims in the manuscript. These experiments are described below as a point-by-point reply to each point raised by the reviewers.

      In line with the aforementioned rationale, we propose the title of our manuscript to change into “Two SATB1 isoforms display different phase separation propensity”, if our manuscript is considered for publication.

      1. Description of the planned revisions

      **Reviewer #1**:

      4) Lack of in vitro reconstitution experiments with purified long and short SATB1

      **PLANNED EXPERIMENT #1**

      We do realize this shortcoming of our work. We have to note that purifying recombinant SATB1 protein is quite a challenging task, yet we 1. cloned both Satb1 cDNAs for the long and short isoforms, 2. we successfully expressed both proteins in great quantity and quality and we are willing to perform these experiments if our work is considered for publication.

      This proposed experiment has also been requested by Reviewers #2 and #3.

      **Reviewer #2**:

      1. Moreover, an important and direct experiment would be to clone the long isoform in a suitable vector and overexpress in the cell line (as done for the canonical isoform in Supp Fig 1a). This would unequivocally show the efficacy of the antibody and thus the following usage of the same for various assays.

      **PLANNED EXPERIMENT #2**

      This is a great suggestion. We have cloned the long and short Satb1 cDNAs in pEGFP-C1 vector. We will transfect these plasmids in NIH 3T3 fibroblasts and we will perform Western blot analysis, utilizing the antibody raised against the extra 31 amino acids long peptide present only in the long SATB1 isoform, for the following samples: 1. NIH-3T3 whole cell protein extracts, 2. protein extracts from NIH 3T3 fibroblasts transiently transfected with the pEGFP-C1 plasmid, 3. protein extracts from NIH 3T3 fibroblasts transiently transfected with the pEGFP-long_Satb1_ plasmid and 4. protein extracts from NIH 3T3 fibroblasts transiently transfected with the pEGFP-short_Satb1_ plasmid.

      This experiment will consist another proof regarding the specificity of the antibody raised against the extra 31 amino acids long peptide present only in the long SATB1 isoform.

      **Minor comments:**

      1. On pg 6, related to Figure 1, the authors mention 'It should also be noted that when investigating the SATB1 protein levels, we have to bear in mind that the antibodies targeting the N-terminus of SATB1 protein cannot discriminate between the short and long isoforms'. The authors reason that their sizes are too close. It is indeed possible, and widely studied in biochemistry to assess various factors on protein migration (such as PTMs). The authors should validate this aspect (as it is important as per their premise) and perform separation based on charge as well and also use a commercial antibody to validate the same.

      (Experiments already performed)

      We have adapted the text so that it does not imply that the two isoforms cannot be separated by size. This part in lines 102-107 then reads: “It should also be noted that when investigating the SATB1 protein levels, we have to bear in mind that the antibodies targeting the N-terminus of SATB1 protein cannot discriminate between the short and long isoforms, thus we can only compare the amount of the long SATB1 isoform to the total SATB1 protein levels in vivo conditions. To overcome this limitation and to specifically validate the presence of the long SATB1 protein isoform in primary murine T cells, we designed a serial immunodepletion-based experiment (Fig. 1e, Supplementary Fig. 1a).”

      Moreover, in the revised version of the manuscript we now provide a number of additional proofs supporting the presence of the long isoform and also the specificity of the long isoform-specific antibody. As evident in the text cited above, in the revised Fig. 1e,f and revised Supplementary Fig. 1a,b; we present two immunodepletion experiments which should alone address the Reviewer’s concerns. Moreover, we added Supplementary Fig. 1c; demonstrating that the long isoform-specific antibody does not detect any protein in cells with conditionally depleted SATB1 (Satb1_fl/fl_Cd4-Cre+), supporting its specificity. The custom-made and publicly available antibodies targeting all SATB1 isoforms were also verified in Supplementary Fig. 1d. Moreover, the long isoform and all isoform antibodies display similar localization in the nucleus (Supplementary Fig. 1e; their co-localization based on super-resolution microscopy is also quantified in Supplementary Fig. 5a).

      In our accompanying revised manuscript Zelenka et al., 2022 (https://doi.org/10.1101/2021.07.09.451769), we will provide yet another piece of evidence, consisting of bacterially expressed short and long SATB1 protein isoforms detected by western blot using either the long isoform-specific or the non-selective all SATB1 isoform antibodies.

      **PLANNED EXPERIMENT #3**

      Although we think that in the revised version of the manuscript, we have provided enough proof about the existence of the long isoform in primary murine thymocytes we would like to try the following approach as suggested by this Reviewer.

      The pI of the two SATB1 isoform is quite similar. The pI of the short SATB1 isoform is 6.09 and for the long SATB1 isoform is 6.18. We will perform 2D PAGE coupled to Western blotting utilizing the antibodies detecting the long and all SATB1 isoforms. Given the fact that both isoforms are post-translationally modified to a various degree, it will be extremely difficult to discriminate between the long and short unmodified versus the long and short post-translationally modified proteins especially in the absence of a specific antibody only for the short isoform.

      **Reviewer #3**

      1. Hexanediol is another assay frequently used in phase-separation studies. However, hexanediol has many deleterious effects on the cell, even at a fraction of the concentration normally used in phase-separation studies. Authors should show controls of cell viability, control proteins that do not phase-separate, etc. See https://www.jbc.org/article/S0021-9258(21)00027-2/fulltext.

      Secondly, hexanediol treatment should cause phase-separated protein aggregates to disperse. It is difficult to determine from the images whether or not the aggregates actually disperse or there is just less protein. In any case, small aggregates remain even after treatment, and this appears different from most other hexanediol experiments reported in the literature where the signals become more dispersed and uniform. This is likely because the samples are fixed.

      One of the main features of using hexanediol in phase-separation is to show that upon washout, LLPS aggregates can reform. Because the cells are fixed, the critical aspect of this assay is not performed. A washout and LLPS recovery would control for cell viability issues described above and would provide the opportunity to show that total SATB1 protein levels did not change, but its distribution did, which is the essence of this assay in the context of LLPS. This review from the Tjian group is very informative and may be a good resource:

      http://genesdev.cshlp.org/content/33/23-24/1619

      In line with our reply to point #1 of this Reviewer (page 26 of this document), we should again emphasize that we utilized the hexanediol treatment in primary murine developing T cells as this is the only way to investigate the properties of SATB1 speckles under physiological conditions. This also explains why some small insoluble structure remains after the hexanediol treatment. Note that under physiological conditions, there is a contribution of several protein variants (such as differential PTMs) out of which some will tend to form more stable structures while others could undergo LLPS. It is not clear how the washout experiment could be applied in the primary cell conditions that include cell fixation as the heterogeneity and big variation among cells would make such data analysis highly unreliable.

      **PLANNED EXPERIMENT #1**

      As we answered to point #4 of Reviewer 1 (page 2), we propose the following experiment. Although the purification of recombinant SATB1 protein is quite a challenging task, yet we 1. cloned both Satb1 cDNAs for the long and short isoforms, 2. we successfully expressed both proteins in great quantity and quality and we are willing to perform in vitro reconstitution experiments if our work is considered for publication.

      1. The major difference between the long and short isoform of SATB1 is the 31aa segment within the IDR. However the authors find that neither the long or short isoform SATB1 forms LLPS aggregates, and the IDR alone forms aggregates in the cytoplasm (Fig5) but they do not respond to Cry2 light activation. When forced to localize to the nucleus, it does not form aggregates as well (Fig6). The short isoform also did not form any aggregates. These results seem to argue against any isoform specific phase-separation. This experiment seems critical for the story, yet it does not support their overall conclusions. The authors might consider using a different cell line or perhaps do an in vitro assay using purified protein.

      I am not certain what to make of the cytoplasmic aggregation, which appears to not form upon localization to the nucleus. Because of this, it is difficult to place weight on the significance of the S635A mutation and the role that a phosphorylation of SATB1 contributes to phase-separation, let alone function There are many additional points of concern, but the ones listed above are perhaps the most significant in terms of the overall conclusions of the paper.

      In Fig. 5c we show that the full length long SATB1 isoform often aggregates unlike the short isoform. These data are accompanied with the results for the IDR region, where the situation is even more obvious (Fig. 5f,g). However, in the latter, we have to bear in mind the absence of the multivalent N-terminal part of the protein which seems to be essential for the overall phase behavior of the protein as indicated in Fig. 4b,c.

      **PLANNED EXPERIMENT #1**

      To further support LLPS of SATB1, we are considering performing the following in vitro experiment, as we answered to point #4 of Reviewer 1 (page 2). Although the purification of recombinant SATB1 protein is quite a challenging task, yet we 1. cloned both Satb1 cDNAs for the long and short isoforms, 2. we successfully expressed both proteins in great quantity and quality and we are willing to perform in vitro reconstitution experiments if our work is considered for publication.

      1. Description of the revisions that have already been incorporated in the transferred manuscript

      **Reviewer #1 (Evidence, reproducibility and clarity)**:

      This paper looks at an important nuclear matrix protein SATB1, which is a well known global chromatin organizer and help chromatin loop attach to the nuclear matrix. The paper starts with identification of novel short and long form of SATB1. Both the isoform consist of a prion like low complexity domains, but the long isoform additionally contain an extra EPF domain next the Prion like low complexity domain. The paper reports that in murine cells the long isoform is 3-4 fold more abundant than the short isoform. By using STED microscopy they show SATB1 foci lie next to transcription sites in the nucleus. They conclude by looking at the spherical shape of the SATB1 foci and the susceptibility of SATB1 staining after 1,6 hexanediol treatment that SATB1 forms the small foci in the nucleus due to LLPS. The authors also use RAMAN spectroscopy to conclude a change in nuclear chemical space in absence of SATB1 but without much explanation about which chemical bond or nuclear sub structure change correspond to the change in principal component analysis from Raman spectroscopy. The authors use the light inducible aggregation cry2 tag with the PrD domain of SATB1 and compare it with the Cry2-FUS-LC domain to conclude that the SATB1 LC domain can undergo LLPS. The authors hint at involvement of RNA and also DNA in the LLPS of the SATB1 but without going into any detail. Reviewer: The paper reports that in murine cells the long isoform is 3-4 fold more abundant than the short isoform.

      Actually, in page 5 (lines 94-96) of the manuscript we write: “We confirmed that in murine thymocytes the steady state mRNA levels of the short Satb1 transcripts were about 3-5 fold more abundant compared to the steady state mRNA levels of the long Satb1 transcripts (Fig. 1d).” Although the steady state mRNA levels of the long isoform are less abundant compared to the shorter isoforms, the long isoform protein levels are almost comparable to the short isoform as deduced based on immunofluorescence experiments. Moreover, Using our two immunodepletion experiments we quantified the difference, estimating the long isoform being 1.5× to 2.62× less abundant than the short isoform (Fig. 1f and Supplementary Fig. 1b; compare lanes 2 & 3 at the lower panel). • Regarding the RAMAN spectroscopy experiments please see Minor Comment #1 of this Reviewer (page 10).

      The key conclusions of the paper are- A) SATB1 undergoes LLPS. But this conclusion is drawn after correlative experiments as detailed below-

      This conclusion is indeed made based on correlative experiments only for the primary murine T cells, which do not allow for any targeted experiments. However, the use of in vitro cell lines allowed us to validate these findings using the optogenetic approaches, utilizing additional experimentation.

      1) observation of spherical punctae by STED-which could also seem spherical due to their small size. The resolution limit achieved by the STED microscopy used in this paper is not determined or mentioned clearly.

      In the revised version of the manuscript, we have specified the resolution of our systems, for STED in Lines 745-746: ”This system enables super-resolution imaging with 35 nm lateral and 130 nm axial resolution.” and for SIM in Lines 759-761: “Images were acquired over the majority of the cell volume in z-dimension with 15 raw images per plane (five phases, three angles), providing ~120-135 nm lateral and ~340-350 nm axial resolution for 488/568 nm lasers, respectively.” The size of the observed speckles is thus above the resolution limit with sizes ranging between 40-80 nm.

      The resolution of our systems is routinely verified by the following methods: The resolution of our OMX (SIM-3D) system was tested using ARGO-SIM slide containing a pattern of 36 µm long lines with gradually increasing spacing ranging from (left to right) 0 to 390 nm, with a step of 30 nm (Fig. 1 below). Our SIM system was able to clearly resolve two lines separated by 120 nm.

      2) No live cell FRAP experiment with fluorescent SATB1 long or short isoform to show that these foci are liquid like

      We did perform FRAP experiments for the SATB1 N-terminus optogenetic construct as demonstrated in Fig. 4f. We did not perform FRAP in the primary murine T cells as this is not technically feasible without creating a new mouse line with fluorescently labeled protein. In the revised version of the manuscript, we additionally performed FRAP experiments for the full length short and long isoform of SATB1 labeled with EGFP and transfected into the NIH-3T3 cell line (Supplementary Figure 6f).

      5) LLPS is strongly coupled to the cellular concentration of the proteins. Authors should quantify the cellular concentration of the long and short isoform in the cells.

      We did consider protein concentration in our analyses of optogenetic constructs in Fig. 4b,d,e and Supplementary Fig. 6a,b,c. Quantifying the physiological cellular concentration of short and long SATB1 protein isoforms in primary T cells is impossible due to the inherent inability to discriminate between the isoforms by two antibodies, in the absence of Satb1 isoform-specific knockout mice.

      However, an approximation of the cellular concentration can be obtained from our immunodepletion experiments. On top of the original immunodepletion experiment that we now present in Supplementary Fig. 1a,b; in the revised version of the manuscript we have repeated the experiment in Fig. 1e,f. Comparison of the two bands for the long and short SATB1 isoforms in the lower panel of the western blot figures suggest that the long SATB1 isoform protein levels are 1.5× to 2.62× less abundant than the short isoform, according to the original and new immunodepletion experiment, respectively. This is now also included in the main text in Lines 110-116: “This experiment can also be used for approximation of the cellular protein levels of SATB1 isoforms in primary murine thymocytes. Comparison of the two bands for long (lane 2) and short SATB1 (lane 3) isoform in the lower panel of Fig. 1f and Supplementary Fig. 1b, suggests that the long SATB1 isoform protein levels may be about 1.5× to 2.62× less abundant than the short isoform, according to the two replicates of our immunodepletion experiment, respectively.”

      Major conclusion B)- SATB1 regulates transcription and splicing.

      This was also shown previously and in this paper they show the close proximity of the transcription site and SATB1 foci by microscopy. Hexanediol treatment which lead to loss of colocalization between FU foci and SATB1 is also taken as an evidence in regulation of transcription is not right as the transcription foci itself can be dissolved using 1,6 Hexanediol. Although the rate of transcription is not measured quantitatively.

      As mentioned in comment #3 (page 29) of this Reviewer, unfortunately there is no better tool to investigate these questions in primary cells than using microscopy approaches in conjunction with hexanediol treatment. However, we should also note that there is an accompanying manuscript from our group that is currently being under revision in another journal (preprint available: Zelenka et al., 2021; https://doi.org/10.1101/2021.07.09.451769). In the preprint manuscript, we showed that: 1. the long SATB1 isoform binding sites have increased chromatin accessibility than what expected by chance (Fig. 3b), 2. there is a drop in chromatin accessibility at SATB1 binding sites in Satb1 cKO mouse (Fig. 3c) and 3. this drop in chromatin accessibility is especially evident at the transcription start sites of genes (Supplementary Fig. 1i)

      We believe that, together these data suggest a direct involvement of SATB1 in transcription regulation. Also note the vast transcriptional deregulation that occurs in Satb1 cKO T cells, affecting the expression of nearly 2000 genes (Fig. 2f, this revised manuscript). That is why we believe that the co-localization analysis, using super-resolution microscopy, presented in Fig. 2c and quantified in Fig. 3g, represents a nice additional support to our claims. Moreover, in the revised version of the manuscript we now present a positive correlation between SATB1 binding and deregulation of splicing (Supplementary Fig. 4d) which also supports its direct involvement in the regulation of transcriptional and co-transcriptional processes.

      In the revised version of the manuscript we have made this clear in Lines 182-194: “Satb1 cKO animals display severely impaired T cell development associated with largely deregulated transcriptional programs as previously documented19,37,38. In our accompanying manuscript19, we have demonstrated that long SATB1 isoform-specific binding sites (GSE17344619) were associated with increased chromatin accessibility compared to randomly shuffled binding sites (i.e. what expected by chance), with a visible drop in chromatin accessibility in Satb1 cKO. Moreover, the drop in chromatin accessibility was especially evident at the transcription start site of genes, suggesting that the long SATB1 isoform is directly involved in transcriptional regulation. Consistent with these findings and with SATB1’s nuclear localization at sites of active transcription, we identified a vast transcriptional deregulation in Satb1 cKO with 1,641 (922 down-regulated, 719 up-regulated) differentially expressed genes (Fig. 2f). Specific examples of transcriptionally deregulated genes underlying SATB1-dependent regulation are provided in our accompanying manuscript19. Additionally, there were 2,014 genes with altered splicing efficiency (Supplementary Fig. 4d-e; Supplementary File 3-4). We should also note that the extent of splicing deregulation was directly correlated with long SATB1 isoform binding (Supplementary Fig. 4d).”

      Major conclusion C)-Post transcriptional modification is important for SATB1 function.

      This point is just barely touched upon in the last figure of the paper

      We would not call the identification of the novel phosphorylation site as a main conclusion of our manuscript. Though, it is already known that posttranslational modifications of SATB1 are important for its function as they can function as a molecular switch rendering SATB1 into either an activator or a repressor (Kumar et al., 2006; https://doi.org/10.1016/j.molcel.2006.03.010).

      In the revised manuscript, we support the effect of serine phosphorylation on the DNA binding capacity of SATB1 by another experiment. We have performed DNA affinity purification experiments utilizing primary thymocyte nuclear extracts treated with phosphatase (Supplementary Fig. 7b). We found that SATB1’s capacity to bind DNA (RHS6 hypersensitive site of the TH2 LCR) is lost upon treatment with phosphatase (Supplementary Fig. 7c). These results are in line with the data presented in Supplementary Fig. 7d, indicating the lost ability of SATB1 to bind DNA upon mutating the discovered phosphorylation site S635. Given the importance of posttranslational modifications of proteins on LLPS, we found it relevant to include it in our manuscript. Even more so, when we identified SATB1 aggregation, upon mutation of this phospho site (Fig. 6d).

      Overall I find that the major conclusion-point A and B, is based on very indirect experiments and needs much more convincing data and the role of SATB1 LLPS in cells should be demonstrated more rigorously. And conclusion C is barely described and needs a lot more cell biological and genetic evidence.

      One of the major assets of our work is that most of our data are based on the analysis of primary murine T cells and thus investigating the biological roles of the endogenous SATB1 protein, under physiological conditions. We apologize that we did not make it clear to this Reviewer, that our system has certain inherent limitations due to the utilization of primary cells.

      I do not recommend publishing the paper in current state. The story needs much more experiment to convincingly prove the major conclusions. Further, the MS needs more careful thinking and presentation to make it streamlined.

      We hope that in the revised version we have significantly improved the quality of our manuscript by implementing the suggested changes.

      Minor comments: One of the major flaw of the paper is the use too many techniques without proper explanation. E.g. use of STED and RAMAN microscopy need controls and explanation on what is being quantified. The use of Raman microscopy to quantify the nuclear environment of nucleus is not related to the chromatin organization or LLPS of SATB1 at all. And no information is provided at all which aspect of nuclear organization is being measured in Raman and what it means for the LLPS of SATB1.

      We do provide quite a thorough explanation of Raman spectroscopy and the underlying quantification in Lines 224-231: “we employed Raman spectroscopy, a non-invasive label-free approach, which is able to detect changes in chemical bonding. Raman spectroscopy was already used in many biological studies, such as to predict global transcriptomic profiles from living cells42, and also in research of protein LLPS and aggregation43–47. Thus we reasoned that it may also be used to study phase separation in primary T cells. We measured Raman spectra in primary thymocytes derived from both WT and Satb1 cKO animals and compared them with spectra from cells upon 1,6-hexanediol treatment. Principal component analysis of the resulting Raman spectra clustered the treated and non-treated Satb1 cKO cells together, while the WT cells clustered separately (Fig. 3h).” We also do provide controls as the method was performed on both treated and untreated WT and Satb1 cKO cells.

      Regarding the RAMAN spectroscopy experiments we now provide more information on the changes of chemical bonds altered between wild type and Satb1 cKO thymocytes. Following principal component analysis, we have extracted the two main principal components that were used for the clustering of our data. The differences are presented in Supplementary Fig. 5d.

      We do realize that RAMAN spectroscopy, although a quite novel approach utilized to study LLPS, has not been used to study LLPS in live cells. If deemed proper we are willing to avoid presenting these results in this manuscript.

      Similarly for Hexanediol treatment, duration of treatment is missing. Hexanediol can also dissolve the liquid like transcription foci. And hence a decrease in correlation between SATB1 foci and FU foci cannot be taken as a measure of SATB1 foci connection to transcription alone

      The duration of hexanediol treatment was 5 minutes as presented in Line 724 and in the revised version of the manuscript also in Lines 1206-1207. We should also note that additionally, we performed experiments with different hexanediol concentrations and timing varying from 1 minute to 10 minutes with results consistent with the data presented.

      It is not very clear how many times the STED or Raman microscopy is done on how many samples and biological replicates. Similarly for RNA sequencing number of samples and description of controls are missing. Also if the sequencing data is made publicly available is not clear.

      Data availability is clearly stated in Lines 506-509: “RNA-seq experiments and SATB1 binding sites are deposited in Gene Expression Omnibus database under accession number GSE173470 and GSE173446, respectively. The other datasets generated and/or analyzed during the current study are available upon request.”

      The Reviewer’s token is “wjwtmeeeppovzqx”.

      RNA sequencing was performed in a biological triplicate for each genotype as stated in the GEO repository and now also in Line 566 of the revised manuscript.

      In Lines 180-181, we also state that it was performed on Satb1 cKO animals and WT mice as a control: “we performed stranded-total-RNA-seq experiments in wild type (WT) and Satb1fl/flCd4-Cre+ (Satb1 cKO) murine thymocytes”.

      In Lines 739-740, we now also state that all imaging approaches were performed on at least two biological replicates (different mice) and please also note the fact that all findings were based on data from both STED and 3D-SIM methods, allowing to minimize detection of artifacts. In the Raman spectroscopy figure, each point represents measurements from an individual cell and for each condition we used 2-5 biological replicates (Lines 831-832 & Line 1169).

      Similarly, in Lines 129-132 we provided a quite detailed description of differences between STED and 3D-SIM, even though these techniques are not that rare as Raman spectroscopy in biology research.

      Additional control is needed to report the resolution limit of Superresolution techniques-STED and 3D-SIM systems used by them.

      We have already provided this information in our reply to comment #1 of this Reviewer (pages 6-7): In the revised version of the manuscript, we have specified the resolution of our systems, for STED in Lines 745-746: ”This system enables super-resolution imaging with 35 nm lateral and 130 nm axial resolution.” and for SIM in Lines 759-761: “Images were acquired over the majority of the cell volume in z-dimension with 15 raw images per plane (five phases, three angles), providing ~120-135 nm lateral and ~340-350 nm axial resolution for 488/568 nm lasers, respectively.” The resolution of our systems is routinely verified by the following methods: The resolution of our OMX (SIM-3D) system was tested using ARGO-SIM slide containing a pattern of 36 µm long lines with gradually increasing spacing ranging from (left to right) 0 to 390 nm, with a step of 30 nm (Fig. 1 below). Our SIM system was able to clearly resolve two lines separated by 120 nm.

      Would be very helpful if the zonation was plotted for the FluoroUridine (FU) also to show that Zone1 (heterochromatin) is completely depleted of FU, and is present in other regions.

      In the revised version of the manuscript, we performed the suggested analysis and in Supplementary Fig. 3a we now show that indeed FU is significantly less localized to Zone 1 (heterochromatin) and has the most abundant localization in Zones 3 and 4, similar to the localization of SATB1 protein, as demonstrated in Fig. 2b.

      Scale bar needed figure 3d

      In the revised version of the manuscript, we included scale bars which are both 0.5 µm (line 1213).

      Perfectly rounded SATB1 foci- this does not mean LLPS. For LLPs measurement, protein condensate dynamics measurement by FRAP or fusion experiments is required. What is the size of condensates? and cellular concentration of SATB1? Will SATB1 undergo LLPS in vitro at similar concentrations? does SATB1 interact with DNA or RNA to undergo LLPS ?

      We toned down this sentence which now reads: “Here we demonstrated its connection to transcription and found that it forms spherical speckles (Fig. 1g), markedly resembling phase separated transcriptional condensates. (Lines 200-202)”.

      Moreover, as explained in earlier replies to comments of this Reviewer, we cannot perform FRAP on primary murine T cells without generating a new mouse line. We did, however, use FRAP and other in vitro approaches including visualization of droplet fusion in ex vivo experiments utilizing cell lines. Moreover, we are willing to demonstrate the LLPS properties of SATB1 on in vitro purified SATB1 protein as indicated in the suggested experiment of Point#4 (page 2).

      After careful reading of the MS I conclude that the main conclusions of the paper are very preliminary and need much more detailed experiments. So does not qualify to get published at all at this stage.

      **Reviewer #1 (Significance)**:

      The present manuscript tries to connect the phase separation of SATB1 to understanding the mechanism of SATB1 function in cells. One of the major hallmarks of phase separation is dynamic, liquid-like behaviour and in absence of these measurements, it is very difficult to say that the current manuscript has made any contribution to showing that SATB1 can phase separate.

      The presence of 2 isoforms of SATB1 is a novel finding and the paper could have focused more on this. E.g. elucidate expression of the isoform during thymocyte development and maturation.

      As a reviewer my expertise are cell biology experiments, microscopy, in vitro reconstitution assays, RNA binding proteins, RNA and RBP condensate formation. And I feel that the reconstitution experiments are an important tool for understanding phase behaviour of proteins and also to gauge if this behaviour can occur or not in cellular concentration and conditions.

      I do not have sufficient expertise in Raman microscopy and hence the information provided in the MS on this part was not enough to understand the experiment and conclusions drawn from it.

      **Reviewer #2 (Evidence, reproducibility and clarity)**:

      The authors have reported the existence of a 'long' SATB1 isoform which also undergoes LLPS. The authors tried to draw multiple comparisons and pointed out distinction between phase properties of SATB1 isoforms. The authors also touch upon two functional roles of SATB1. Although a wide array of assays are used, the data presented and hence the manuscript makes multiple transitions into disparate hypotheses without diving deep into a single hypothesis. As a result, the connections drawn are unclear, and do not converge at best. The authors have used number of techniques, however, the results do not support their conclusions and they appear hastily drawn. It is not clear why the authors jump from one context to the other, discussing LLPS first, then transcription, splicing, post-translational modification and finally cancer. The link between all of these isn't clear and not fully supported by data. It appears that the authors wish to focus on Satb1's physiological role in development, hence the data on breast cancer is confusing. Thus, this work suffers from multiple pitfalls. Specific comments are given below:

      Major comments 1. Importantly, in Fig 1d, there is no statistics shown. There is no mention of number of replicates as well in the legends. Proper statistical evaluation is critical for interpreting this result.

      Please note that Fig. 1d only serves as a control to the sequencing experiment in Fig. 1b. In Line 566, we now state that for the RNA-seq: “A biological triplicate was used for each genotype.” To validate these data, we further designed a RT-qPCR experiment which was performed on three technical replicates from a male and female mouse. We now state this in Line 636. For the low number of samples, statistical tests are not accurate but we still added t test into the figure Fig. 1d and specified it also in the figure legend in Line 1169-1170.

      1. Figure 1f presents one of the weakest evidences in the manuscript. There are a number of corrections needed. Firstly, being their major and only validation figure for their custom antibody, the immunoblot is not clean, bands are fuzzy. Importantly, as the authors claim that the antibody is highly specific to 'long' SATB1, after the IP there should be only a single band (like input) of Satb1 long. But that does not seem to be the case, rather an array of bands are visible below (lane 2 top panel). This could easily mean that the shorter isoforms or non-specific protein bands are also pulled down with the 'long' form specific antibody. Therefore, raising a critical concern regarding the specificity of the antibody.

      • The long antibody was raised in mice inoculated with the extra peptide present in the long isoform only. Therefore, the capacity of this antibody precipitating the shorter isoforms, which do not express the sequence of the extra peptide (EP, Figure 1a) in not possible. • We have repeated the immunodepletion experiment and we now provide the results in Fig. 1f and Supplementary Fig. 1b. The western blot in Fig. 1f is now cleaner and supports quite convincingly the presence of a long SATB1 isoform. Given the lack of isoform-specific knockouts which we could utilize to immunoprecipitate or detect the different isoforms in a single cell (or cell population), the utilized approach of immunodepletion and subsequent western blotting is the approach we thought of implementing. • As shown in Fig. 1f and Supplementary Figure 1b, the long isoform SATB1 antibody has the capacity to recognize the long isoform in murine thymocyte protein extracts but not the short SATB1 isoform (please compare lane 3 in the two western blots utilizing either the antibody for the long isoform -top panel - or the antibody that detects both isoforms (lower panel). • We have performed Immunofluorescence experiments utilizing the antibody detecting the long SATB1 isoform in thymocytes isolated from either C57BL/6 or Satb1 cKO mice. The antibody is specific to the SATB1 protein since there is no signal in immunofluorescence experiments utilizing the knockout cells (Supplementary Figure 1c). • We have performed Immunofluorescence experiments utilizing thymocytes and the antibody detecting the long SATB1 or a commercially available antibody detecting all SATB1 isoforms. The pattern of SATB1 subnuclear localization is similar for both antibodies (Supplementary Figure 1e). • In our accompanying revised manuscript Zelenka et al., 2022 (https://doi.org/10.1101/2021.07.09.451769), we provide yet another piece of evidence, consisting of bacterially expressed short and long SATB1 protein isoforms detected by western blot using either the long isoform-specific or the non-selective all SATB1 isoforms antibodies. • Regarding the additional bands detected in the immunoprecipitation experiment presented in the original Supplementary Figure 1b (lane 2), it is not surprising that additional bands appear in a sample of protein extracts that is used for several hours for the immunoprecipitation experiments, while the “input” sample simply denotes protein extract that is frozen at -80oC right after the preparation of protein extracts until use. It is well-established that SATB1 is the target of proteases which might as well be active during the immunoprecipitation steps (2 consecutive immunoprecipitation steps take place). Therefore, the immunoprecipitated material cannot necessarily be a copy of the input material displaying a single protein band even if protease inhibitors are included in the buffers.

      Taken together the experiments described here we showed that the antibody raised against the extra 31 aa long peptide, present only in the long SATB1 isoform, is specific for this isoform.

      1. Related to Fig. 2 a, the authors state on Pg 5, '....the euchromatin and interchromatin regions (zones 3 & 4, Fig. 2a, b).' Although the DAPI correlation seems clear, there is no mention on how they reached the above said correlation. They should at least show a parallel speckle staining for HP1 or signature modification such as H3K4me9 STEDs for making supporting such a claim. DAPI alone is not sufficient. The authors should rectify the text thoroughly for many such interpretations without validation/reference or provide relevant data.

      This is a great suggestion we have again taken under consideration and we added the following experiments and the appropriate changes in the revised version of our manuscript. • We modified the text and added a reference to Miron et al., 2020 (https://doi.org/10.1126/sciadv.aba8811) supporting our claims regarding SATB1 localization in relation to DAPI staining. • We have also added new microscopy images for HP1, H3K4me3 and fibrillarin staining and quantified the localization of FU-stained sites of active transcription in nuclear zones, to further support our claims. • This whole modified part in Lines 139-167 then reads: “ “The quantification of SATB1 speckles in four nuclear zones, derived based on the relative intensity of DAPI staining, highlighted the localization of SATB1 mainly to the regions with medium to low DAPI staining (zones 3 & 4, Fig. 2a, b). A similar distribution of the SATB1 signal could also be seen from the fluorocytogram of the pixel-based colocalization analysis between the SATB1 and DAPI signals (Supplementary Fig. 2a). SATB1’s preference to localize outside heterochromatin regions was supported by its negative correlation with HP1β staining (Supplementary Fig. 2b). Localization of SATB1 speckles detected by antibodies targeting all SATB1 isoforms and/or only the long SATB1 isoform, revealed a significant difference in the heterochromatin areas (zone 1, Fig. 2b), where the long isoform was less frequently present (see also Fig. 2a and Fig. 3c). Although, this could indicate a potential difference in localization between the two isoforms, due to the inherent difficulty to distinguish the two based on antibody staining, we refrain to draw any conclusions. The prevailing localization of SATB1 corresponded with the localization of RNA-associated and nuclear scaffold factors, architectural proteins such as CTCF and cohesin, and generally features associated with euchromatin and active transcription32. This was also supported by colocalization of SATB1 with H3K4me3 histone mark (Supplementary Fig. 2c), which is known to be associated with transcriptionally active/poised chromatin. Given the localization of SATB1 to the nuclear zones with estimated transcriptional activity32 (Fig. 2b, zone 3), we investigated the potential association between SATB1 and transcription. We unraveled the localization of SATB1 isoforms and the sites of active transcription labeled with 5-fluorouridine. Sites of active transcription displayed a significant enrichment in the nuclear zones 3 & 4 (Supplementary Fig. 3a), similar to SATB1. As detected by fibrillarin staining, SATB1 also colocalized with nucleoli which are associated with active transcription and RNA presence (Supplementary Fig. 3b). Moreover, we found that the SATB1 signal was found in close proximity to nascent transcripts as detected by the STED microscopy (Fig. 2c). Similarly, the 3D-SIM approach indicated that even SATB1 speckles that appeared not to be in proximity with FU-labeled sites in one z-stack, were found in proximity in another z-stack (Supplementary Fig. 3c). Additionally, a pixel-based colocalization of SATB1 and sites of active transcription is quantified later in the text in Fig. 3g, supporting their colocalization.”

      1. The authors mention, '...of the different SATB1 isoforms, uncovered by the use of the two different antibodies, relied in the heterochromatin areas (zone 1), where the long isoform was less frequently...' There is no supporting figure number mentioned. The authors need to show a zone-by-zone comparison images for 'all iso' vs 'long' iso of SATB1. Just to reiterate, there is a need for a heterochromatin mark to unambiguously call out the distinction.

      We should remind that there is an inherent difficulty to accurately compare localization of short and long SATB1 isoforms in primary cells, especially due to the lack of Satb1 isoform-specific knockout mice. There is no way to detect only the short isoform in these primary cells as there are only antibodies targeting the long or all SATB1 isoforms. Therefore, we cannot set up additional experiments probing these questions.

      In line with this, in the revised version of the manuscript, we toned down our statements regarding the differential localization of the two isoforms in primary cells. We only refer to it as an indication and we support it by adding references to the relevant figures. This part now reads: “Localization of SATB1 speckles detected by antibodies targeting all SATB1 isoforms and/or only the long SATB1 isoform, revealed a significant difference in the heterochromatin areas (zone 1, Fig. 2b), where the long isoform was less frequently present (see also Fig. 2a and Fig. 3c). Although, this could indicate a potential difference in localization between the two isoforms, due to the inherent difficulty to distinguish the two based on antibody staining, we refrain to draw any conclusions. (Lines 145-150)”

      1. On the same lines, '....Given the localization of SATB1 to the nuclear zones with estimated transcriptional activity (Fig. 2b, zone 3)....' How was the region labelled as transcriptionally active? For the statistical analysis of speckle count for the two antibodies' staining, the claim posited is a bit bigger. This could simply be true for that cell. The authors thus need to statistically analyse the speckle counts for multiple cells. This needs to be done for all imaging statistics done in multiple figures throughout the manuscript.

      As mentioned in our reply to the two previous comments of this Reviewer, transcriptional activity in relation to the nuclear zonation is well established in the literature. To make this clear, we have now added the reference to Miron et al., 2020 (https://doi.org/10.1126/sciadv.aba8811) supporting our claims and additionally we have also included HP1, H3K4me3 and fibrillarin staining and quantification of FU signal in the nuclear zones. Moreover, it is not clear to which particular cell the comment refers to. The presented dots in Fig. 2b represent individual cells and the relative proportions of speckles in each nuclear zone are plotted on the y axis. In the revised version of the manuscript, we added into the figure the number of cells scored and we adapted the figure legend so that it is absolutely clear that we have analyzed multiple cells:

      “Nuclei of primary murine thymocytes were categorized into four zones based on the intensity of DAPI staining and SATB1 speckles in each zone were counted. Images used represented a middle z-stack from the 3D-SIM experiments. The graph depicts the differences between the long and all SATB1 isoforms’ zonal localization in nuclei of primary murine thymocytes. (Lines 1189-1193)”

      1. For figure 2c. the authors have used 5 Fluorouridine for nascent RNA speckles. 5FU is known to have a spread signal type (with strong association to nucleolus as well). This is not the case for the image presented 2c. The authors should resolve this by showing different sets of images.

      Developing and naive T cells are very unique in terms of their metabolic features and thus they should not be directly compared with other cell types. Therefore, we would not expect to see such a spread FU pattern as previously shown for other cell types. Having said that, we could not find any reference publication that utilized super-resolution microscopy to detect localization of FU-stained sites of active transcription in developing primary T cells. However, we performed additional immunofluorescence experiments to demonstrate the colocalization or its lack between SATB1 and HP1 (Supplementary Fig. 2b), H3K4me3 (Supplementary Fig. 2c) and fibrillarin (Supplementary Fig. 3b). Moreover, we provide additional regions of SATB1 and FU staining in Supplementary Fig. 3c. The modified text reads:

      “We unraveled the localization of SATB1 isoforms and the sites of active transcription labeled with 5-fluorouridine. Sites of active transcription displayed a significant enrichment in the nuclear zones 3 & 4 (Supplementary Fig. 3a), similar to SATB1. As detected by fibrillarin staining, SATB1 also colocalized with nucleoli which are associated with active transcription and RNA presence (Supplementary Fig. 3b). Moreover, we found that the SATB1 signal was found in close proximity to nascent transcripts as detected by the STED microscopy (Fig. 2c). Similarly, the 3D-SIM approach indicated that even SATB1 speckles that appeared not to be in proximity with FU-labeled sites in one z-stack, were found in proximity in another z-stack (Supplementary Fig. 3c). Additionally, a pixel-based colocalization of SATB1 and sites of active transcription is quantified later in the text in Fig. 3g, supporting their colocalization. (Lines 157-167)”

      1. Fig 2 d., the authors have suddenly jumped solely to 'all iso' Satb1 here for IP MS. Is there a reason for that? The authors either need to do this with 'long iso' antibody or remove the analysis from the manuscript as it does not add to their primary aim of the manuscript. Also, the authors have only selectively talked about two clusters? What about chromatin related proteins? It is quite intuitive to have highest enrichment of these given previous literature and even IP MS data by other groups. Thus, it is necessary to revise this thoroughly or remove it.

      We appreciate the acknowledgment by the Reviewer that our IP-MS data identified anticipated factors. In the revised version of the manuscript we modified the underlying text to accommodate references to these former findings revealing interactions between SATB1 and chromatin modifying complexes: “Apart from subunits of chromatin modifying complexes that were also detected in previous reports25,33–36, unbiased k-means clustering of the significantly enriched SATB1 interactors revealed two major clusters consisting mostly of proteins involved in transcription (blue cluster 1; Fig. 2d and Supplementary Fig. 4c) and splicing (yellow cluster 2; Fig. 2d and Supplementary Fig. 4c). (Lines 170-174)”

      Please note that many subunits of chromatin modifying and chromatin-related complexes are in fact characterized as transcription-related factors, therefore our statements are not in disagreement with the former findings. Note also that we provide Supplementary File 1 & 2 with comprehensive description of our IP-MS data for the readers’ convenience. Please also note that we are the first group to report on the existence of the long isoform. Therefore, we find it absolutely reasonable to perform IP-MS experiment for all SATB1 isoforms which can then be used for a comparison with other publicly available datasets. We believe that there is no contradiction in this experimental setup in relation to the rest of the manuscript. We discuss the two major clusters simply because they are the two major clusters identified as indicated in Fig. 2d. Additionally, in Supplementary Fig. 4c, we provide a comprehensive description of all significantly enriched interactors including their cluster annotation and thus anyone can investigate the data if needed.

      1. In relation to Fig. 2f, the authors have not mentioned any of the previously published work on Satb1 CD4 specific KO, not even the RNA seq studies the other groups have reported under the same condition. Only an unpublished reference of their own (preprint) is cited. It is imperative to show how much their data corroborates with other published studies. Additionally, what is the binding site status of dysregulated genes?

      In the revised version of the manuscript, we have included the references to other studies using the same Satb1 conditional knockout. Moreover, we have clarified the relationship between SATB1 binding and gene transcription. The modified part in Lines 182-194 now reads: “Satb1 cKO animals display severely impaired T cell development associated with largely deregulated transcriptional programs as previously documented19,37,38. In our accompanying manuscript19, we have demonstrated that long SATB1 isoform specific binding sites (GSE17344619) were associated with increased chromatin accessibility compared to randomly shuffled binding sites (i.e. what expected by chance), with a visible drop in chromatin accessibility in Satb1 cKO. Moreover, the drop in chromatin accessibility was especially evident at the transcription start site of genes, suggesting that the long SATB1 isoform is directly involved in transcriptional regulation. Consistent with these findings and with SATB1’s nuclear localization at sites of active transcription, we identified a vast transcriptional deregulation in Satb1 cKO with 1,641 (922 down-regulated, 719 up-regulated) differentially expressed genes (Fig. 2f). Specific examples of transcriptionally deregulated genes underlying SATB1-dependent regulation are provided in our accompanying manuscript19. Additionally, there were 2,014 genes with altered splicing efficiency (Supplementary Fig. 4d-e; Supplementary File 3-4). We should also note that the extent of splicing deregulation was directly correlated with long SATB1 isoform binding (Supplementary Fig. 4d).”

      1. In context of Figure 3a and b, the authors write .'...The long SATB1 isoform speckles evinced such sensitivity as demonstrated by a titration series with increasing concentrations of 1,6-hexanediol treatment followed...' Whereas it is apparent from the image at least that overall numbers of individual speckles are instead increased at both 2 and 5%. There is although a clear spreading of restricted speckles compared to the controls. The authors should revise their figures to substantiate the associated text. Furthermore, there needs to be 'all iso' SATB1 3D SIM imaging and not just quantitation for comparison. This is also true for panel c in order to demonstrate the effect.

      In the revised Fig. 3a we provide new images which better reflect the underlying data analysis. Moreover, in Fig. 3c and Fig. 3d we provide an additional comparison between SATB1 all isoforms and long isoform staining and their changes upon hexanediol treatment, detected by both the 3D-SIM and STED approaches. It is true that upon treatment, there tend to be more speckles, however these are much smaller as they are gradually being dissolved. Depending on the treatment duration, the cells are swollen which is reflected in increased spreading of speckles. Nevertheless, the nuclear size was considered in all the quantification analyses. We believe that the new images provide better evidence of SATB1’s sensitivity to hexanediol treatment.

      1. Fig. 3 d also does not clearly demonstrate what the authors have claimed '...hexanediol treatment highly decreased colocalization between...' The figure shows at best decreased signal intensity for both SATB1 and FU. We suggest that the authors should give a statistical analysis as well for the colocalization points between the two using multiple source images. Lastly, the two images shown (control and treated), there seems to be a clearly visible magnification difference. The authors should clarify this.

      • In the revised version of the manuscript in Figure 3d, we have provided scale bars, which are both 0.5 µm (line 1213). The difference observed by this Reviewer is actually the main reason why we provided this image. Figure 3d demonstrates that upon hexanediol treatment, the speckles are mostly missing or significantly reduced in size, for both FU and SATB1 staining. • Moreover, the suggested statistical analysis is also provided – in Figure 3e. In Figure 3e, we performed pixel-based colocalization analysis which is a method that allows both quantification and statistical comparison of colocalization between two factors and between different conditions. Please note especially the decreased colocalization between long SATB1 isoform and FU-stained sites of active transcription in the left graph, which is in agreement with our claims in the manuscript. • Moreover, our data are compared to a negative control, i.e. 90 degrees rotated samples, which is a common method in colocalization experiments as described for example in Dunn et al., 2011 (https://doi.org/10.1152/ajpcell.00462.2010). • Additionally, we provide Costes’ P values which are based on randomly scrambling the blocks of pixels (instead of individual pixels, because each pixel’s intensity is correlated with its neighboring pixels) in one image, and then measuring the correlation of this image with the other (unscrambled) image. Please see Costes et al., 2004 (https://doi.org/10.1529%2Fbiophysj.103.038422) for more details.

      1. Figure 3f. The authors show the PC plot for Raman spectroscopy for phase behaviour due to Satb1. The experiment and its related text seems misinterpreted; the authors write...' ese bonds were probably enriched for weak interactions responsible for LLPS that are susceptible to hexanediol treatment. This shifted the cluster of WT treated cells towards the Satb1 cKO cells. However, the remaining covalent bonds differentiated the WT samples from Satb1 cKO cells......' whereas the clusters are clearly far away in 3D for both WT and KO while being closer to their respective treatments. Which is also intuitive given the sensitivity of Raman spectroscopy. Thus, it is more likely to be treatment effect and KO effect as separate. Treatment of WT leads to KO like spectra is far-fetched. Thus, the authors need to show separate PCs and modify their text thoroughly.

      We do not present any 3D graph hence it is not clear what the Reviewer refers to. Please also note that as stated in Lines 817-818, we used a customized Raman Spectrometer. Therefore, this approach allowed us to measure Raman spectra at cellular and even sub-cellular levels. For example, solely by utilizing Raman spectroscopy, we can now distinguish euchromatin and heterochromatin, methylated and unmethylated DNA and RNA, etc. This, together with other reports, such as Kobayashi-Kirschvink et al., 2018 (https://doi.org/10.1016/j.cels.2018.05.015) and Kobayashi-Kirschvink et al., 2022 (https://doi.org/10.1101/2021.11.30.470655), indicate a potential use of Raman in biological research. In our manuscript, we used this method as a supplementary approach, however we do find it noteworthy. We should also emphasize that in the revised Raman spectroscopy Fig. 3h, each point represents measurements from an individual cell and for each condition we used 2-5 biological replicates (Lines 831-832 & Lines 1225-1226). We specifically refer to the principal component 1 (PC1) that differentiates the samples. Therefore, there are certain spectra (representing certain chemical bonding) that allowed us to differentiate between WT and Satb1 cKO. The same type of bonding was then affected when WT samples were treated with hexanediol and we also had controls to rule out the impact of hexanediol on the resulting spectra.

      1. In Fig 4. b, The authors have shown the propensity of SATB1 N terminus to phase separate using different optodroplet constructs. Although the imaging is clear, why are the regions selected not uniform when comparing various constructs?

      We have selected images that would best represent each category. Please note that this was live cell imaging of photo-responsive constructs, thus there are many limitations regarding the area selection. Very often, even the brief time of bright light exposure to localize cells may trigger protein clustering. Upon disassembly, every new light exposure of the same cell then triggers much faster assembly which skews the overall results. It is therefore desired to work fast, while neglecting selection of equally sized cells. Moreover, it is not clear how would the proposed change improve the quality of our manuscript.

      1. Figure 5a, the disassembly should be shown for 'long' SATB1 as well. On pg 13, the authors write '....cytoplasmic protein aggregation has been previously described for proteins containing poly-Q domains and PrLDs..' no reference given.

      • In the revised version of the manuscript, we present the assembly and disassembly for both short and long full length SATB1 optogenetic constructs. To increase clarity, we present the behavior of the short and long isoforms as two separate images in Figure 5a and Figure 5b, respectively. • Moreover, we provided references to the statement regarding aggregation of PrLD and poly-Q-containing proteins in Lines 305-309, which now reads: ”Since protein aggregation has been previously described for proteins containing poly-Q domains and PrLDs8,11,38,39, we next generated truncated SATB1 constructs encoding two of its IDR regions, the PrLD and poly-Q domain and in the case of the long SATB1 isoform also the extra peptide neighboring the poly-Q domain (Fig. 1a and 4a).”

      1. Fig. 5d, Is there an amino-acid specific reasoning to support the authors claim of the phase behaviour due to extra peptide? They need to show a proper control with equal extra (unrelated) peptide to show the specificity. Are the shorter isoform aggregates responsive to light?

      • We have referred to the amino acid composition bias in Fig. 5c. In the revised version of the manuscript, we made this clear by showing the composition bias in the new revised Fig. 5e. The related part of the main text then reads: “Computational analysis, using the algorithm catGRANULE37, of the protein sequence for both murine SATB1 isoforms indicated a higher propensity of the long SATB1 isoform to undergo LLPS with a propensity score of 0.390, compared to 0.379 for the short isoform (Fig. 5d). This difference was dependent on the extra peptide of the long isoform. Out of the 31 amino acids comprising the murine extra peptide, there are six prolines, five serines and three glycines – all of which contribute to the low complexity of the peptide region3 (Fig. 5e).” (Lines 298-304) • Moreover, we should note that the low complexity extra peptide of the long SATB1 isoform directly extends the PrLD and IDR regions as indicated in Fig. 4a and which we now directly state in Lines 304-305: “Moreover, the extra peptide of the long SATB1 isoform directly extends the PrLD and IDR regions as indicated in the Fig. 4a.” • We show in Fig. 4, that the N terminus of SATB1 undergoes LLPS. Since this part of SATB1 is shared by both isoforms, it is reasonable to assume that both isoforms would undergo LLPS. This is also in line with the observed photo-responsiveness of both short and long full length SATB1 isoforms in CRY2 optogenetic constructs in revised Fig. 5a,b, and similar FRAP results for both short and long full length SATB1 isoform constructs transiently transfected in NIH-3T3 cells in the revised Supplementary Fig. 6f. However, the main reason why we think that the difference in LLPS propensity between the isoforms is important is because the long isoform is more prone to aggregate compared to the short isoform, as documented in Fig 5c,f,g and Supplementary Fig. 5f.

      1. Fig 6c., It is important that authors show the data for NLS+short iso data as well to prove their hypothesis.

      As shown in original Figure 5d, the long SATB1 isoform undergoes cytoplasmic aggregation, unlike the short SATB1 isoform (as shown in the same Figure). Therefore, an image of the NLS + short isoform would not be related to our hypothesis. Actually, we wanted to reverse the long SATB1 isoform’s relocation, from the aggregated form in the cytoplasm into the nucleus. Nevertheless, to show the complete picture, in the revised version of the manuscript in Figure 6c, we now provide data for both short and long SATB1 isoforms.

      1. Fig 6d., The authors claim that mutating a specific P site changes the phase behaviour of the 'short iso'. Does it also increase for the long isoform? The authors need to confirm this in order to verify the effect of a single P site outside of oligomerization domain. ...' phosphorylation status; when phosphorylated it remains diffused, whereas unphosphorylated SATB1 is localized to PML bodies....' This being an important premise, thus should be moved to the results text.

      In the revised version of the manuscript, we moved the part regarding PML in the results section, as suggested by the Reviewer. Moreover, we included additional experiments probing the impact of association between PML and two SATB1 full length isoforms on their dynamics. The modified section in Lines 357-368 now reads: “In relation to this, a functional association between SATB1 and PML bodies was already described in Jurkat cells64. We should note that PML bodies represent an example of phase separated nuclear bodies65 associated with SATB1. Targeting of SATB1 into PML bodies depends on its phosphorylation status; when phosphorylated it remains diffused, whereas unphosphorylated SATB1 is localized to PML bodies66. This is in line with the phase separation model as well as with our results from S635A mutated SATB1, which has a phosphorylation blockade promoting its phase transitions and inducing aggregation. To further test whether SATB1 dynamics are affected by its association with PML, we co-transfected short and long full length SATB1 isoforms with PML isoform IV. The dynamics of long SATB1 isoform was affected more dramatically by the association with PML than the short isoform (Supplementary Fig. 7e), which again supports a differential behavior of the two SATB1 isoforms.”

      Moreover, given the localization of the discussed phosphorylation site in the DNA binding region of SATB1 we did test its impact on DNA binding as documented in the revised Supplementary Fig. 7d. Additionally, as we have noted in our answer in Major Comment C of this reviewer, to further support the effect of serine phosphorylation on the DNA binding capacity of SATB1 we have performed DNA affinity purification experiments utilizing primary thymocyte nuclear extracts treated with phosphatase (Supplementary Fig. 7b) We found that SATB1’s capacity to bind DNA (RHS6 hypersensitive site of the TH2 LCR) is lost upon treatment with phosphatase (Supplementary Fig. 7c).

      1. Pg 16,. The authors have tried to explain multiple things (concepts of self-regulation, accessibility) which is quite tangential. There is no inference to Fig 6f., which is showing the opposite to what the authors had postulated. This portion should either be removed or explained with a rationale. The writing also needs to be revised thoroughly in this section. Similarly, the discussion should also be modified.

      The rationale for the original Fig. 6f (revised Fig. 6g) was described in great detail in Lines 330-343 of the original manuscript. It is not clear why the Reviewer assumes that it shows the opposite to our hypothesis. As we explained, the increased accessibility allows faster read-through by RNA polymerase, and thus the exon with higher accessibility is more likely to be skipped. The exact relationship is shown in the revised Fig. 6g where the increased accessibility is associated with the expression of the short isoform, whereas the long isoform expression needs lower chromatin accessibility which allows the splicing machinery to act on the specific exon to be included. We reason that these findings are important and relevant because: 1) we suggest a potential regulatory mechanism for the SATB1 isoforms production. This is highly relevant to this manuscript given the fact that this is the first report on the existence of the long SATB1 isoform, and 2) the differential production of the long/short SATB1 isoforms has a potential relevance to breast cancer prognosis. In the revised version of the manuscript we added Fig. 6f, which now indicates the differential chromatin accessibility in human breast cancer patients and accordingly the expression of the long SATB1 isoform are associated with worse patient prognosis as indicated in Fig. 6h and Supplementary Fig. 8a,b. In the revised version of the manuscript, we substantially modified the text in Lines 374-408, to make the relevance of all these conclusions clear. The modified text now reads: “Therefore, we reasoned that a more plausible hypothesis would be based on the regulation of alternative splicing. In our accompanying manuscript19, we have reported that the long SATB1 isoform DNA binding sites display increased chromatin accessibility than what expected by chance (Fig. 3b in 19), and chromatin accessibility at long SATB1 isoform binding sites is reduced in Satb1 cKO (Fig. 3c in 19), collectively indicating that long SATB1 isoform binding promotes increased chromatin accessibility. We identified a binding site specific to the long SATB1 isoform19 right at the extra exon of the long isoform (Fig. 6e). Moreover, the study of alternative splicing based on our RNA-seq analysis revealed a deregulation in the usage of the extra exon of the long Satb1 isoform (the only Satb1 exon affected) in Satb1 cKO cells (deltaPsi = 0.12, probability = 0.974; Supplementary File 4). These data suggest that SATB1 itself is able to control the levels of the short and long Satb1 isoforms. A possible mechanism controlling the alternative splicing of Satb1 gene is based on its kinetic coupling with transcription. Several studies indicated how histone acetylation and generally increased chromatin accessibility may lead to exon skipping, due to enhanced RNA polymerase II elongation48,49. Thus the increased chromatin accessibility promoted by long SATB1 isoform binding at the extra exon of the long isoform, would increase RNA polymerase II read-through leading to decreased time available to splice-in the extra exon and thus favoring the production of the short SATB1 isoform in a negative feedback loop manner. This potential regulatory mechanism of SATB1 isoform production is supported by the increased usage of the extra exon in the absence of SATB1 in Satb1 cKO (Supplementary File 4). To further address this, we utilized the TCGA breast cancer dataset (BRCA) as a cell type expressing SATB150. ATAC-seq experiments for a series of human patients with aggressive breast cancer51 revealed differences in chromatin accessibility at the extra exon of the SATB1 gene (Fig. 6f). In line with the “kinetic coupling” model of alternative splicing, the increased chromatin accessibility at the extra exon (allowing faster read-through by RNA polymerase) was positively correlated with the expression of the short SATB1 isoform and slightly negatively correlated with the expression of the long SATB1 isoform (Fig. 6f). Moreover, we investigated whether the differential expression of SATB1 isoforms was associated with poor disease prognosis. Worse pathological stages of breast cancer and expression of SATB1 isoforms displayed a positive correlation for the long isoform but not for the short isoform (Fig. 6g and Supplementary Fig. 6c). This was further supported by worse survival of patients with increased levels of long SATB1 isoform and low levels of estrogen receptor (Supplementary Fig. 6d). Overall, these observations not only supported the existence of the long SATB1 isoform in humans, but they also shed light at the potential link between the regulation of SATB1 isoforms production and their involvement in pathological conditions.”

      1. The authors should not draw conclusions based on any data which is not shown '....ed differences in chromatin accessibility at the extra exon of the SATB1 gene (data not shown), suggesting its potential involvement in alternative splicing regulation according to the "kinetic coupling" model...'. This has led to overspeculation and needs correction.

      In the revised version of the manuscript, we included the ATAC-seq data from human breast cancer patients in the revised Fig. 6f. The legend of this figure now reads: “Human TCGA breast cancer (BRCA) patient-specific ATAC-seq peaks51 span the extra exon (EE: extra exon; labeled in green) of the long SATB1 isoform. Note the differential chromatin accessibility in seven selected patients, emphasizing the heterogeneity of SATB1 chromatin accessibility in cancer. Chromatin accessibility at the promoter of the housekeeping gene DNMT1 is shown as a control. (Lines 1281-1285)” Accordingly, we have also modified the main text: “ATAC-seq experiments for a series of human patients with aggressive breast cancer68 revealed differences in chromatin accessibility at the extra exon of the SATB1 gene (Fig. 6f). In line with the “kinetic coupling” model of alternative splicing, the increased chromatin accessibility at the extra exon (allowing faster read-through by RNA polymerase) was positively correlated with the expression of the short SATB1 isoform and slightly negatively correlated with expression of the long SATB1 isoform (Fig. 6g).” (Lines 395-339)”

      Minor comments: 1. On pg 4, the authors state 'Here, we utilized primary murine T cells, in which we have identified two full-length SATB1 protein isoforms.' Whereas only one 'long' isoform is identified and the other is the canonical version. The authors should correct the statement.

      In the revised version of the manuscript, we modified this statement as follows: ”In this work, we utilized primary developing murine T cells, in which we have identified a novel full-length long SATB1 isoform and compared it to the canonical “short” SATB1 isoform.” (Lines 64-66)”

      1. Fig. 1 a , Is there a specific reason to generate a custom-made antibody for 'all' SATB1, using similar regions that are already commercially available. This becomes redundant otherwise, because there is no apparent difference in detection compared to the commercial one (Suppl. Fig 1a). Antibody generation strategy (1a) should be moved to supplementary. Additionally, authors have obtained the custom antibodies from a commercial source, therefore, the text should reflect the same alongside relevant details.

      The custom-made SATB1 antibody targeting the amino-terminal region of the protein has been developed in order to be utilized for detecting the native form of the protein. Unlike commercially available antibodies raised against either short peptides or denatured forms of the protein we have utilized the native form of the amino-terminal part of the protein for raising this antibody. To be honest, this antibody has been raised in order to be utilized in ChIP-seq experiments since no commercially available antibody is of high quality for this approach. Moreover, the original Figure 1a was utilized in order to provide an overview of the SATB1 protein structure which is highly relevant to understand its biophysical properties and not for presenting the strategy for raising a custom-made antibody for SATB1.

      1. Fig 3e: what is the control used here? In their Pearson correlation analysis, there seem to be significant reduction in control sets as well upon treatment. This needs to be clarified.

      We used scans rotated by 90° which served as a negative control, as stated in Line 769: “SATB1 scans rotated by 90° served as a negative control for the colocalization with FU.” Note that this is a commonly used control in colocalization experiments as described for example in Dunn et al., 2011 (https://doi.org/10.1152/ajpcell.00462.2010).

      Additionally, we provide Costes’ P values which are based on randomly scrambling the blocks of pixels (instead of individual pixels, because each pixel’s intensity is correlated with its neighboring pixels) in one image, and then measuring the correlation of this image with the other (unscrambled) image. Please see Costes et al., 2004 (https://doi.org/10.1529%2Fbiophysj.103.038422) for more details. Moreover, it was actually anticipated to see a decrease in colocalization upon hexanediol treatment even in the negative control, as hexanediol significantly reduces both SATB1 and FU speckles as established in Fig. 3a-d.

      1. Pg 10, the authors claim that '..., thus we reasoned that it may also be used to study phase separation...' But there have been numerous reports starting from 2018, which have utilized this technique in corelation to phase behaviour (albeit individual proteins). The authors should include proper citations as they are extending an idea from the same field to their specific need.

      In the revised version of the manuscript, we included relevant citations to support the use of Raman spectroscopy in LLPS research: “Raman spectroscopy was already used in many biological studies, such as to predict global transcriptomic profiles from living cells42, and also in research of protein LLPS and aggregation43–47. Thus we reasoned that it may also be used to study phase separation in primary T cells.” (Lines 225-228)”

      1. For Fig 5b, there should be a comparative image for 'short' isoform.

      In the revised Figure 5c we have included a comparative image for the short SATB1 isoform.

      1. In the context of Figure 5c, the authors claim ...' Note also the higher LLPS propensity of the human long SATB1 isoform compared to the murine SATB1...' Why suddenly human and mouse comparisons are drawn? This figure should be moved to supplementary.

      The comparison between the human and mouse SATB1 isoforms has been implemented because it is relevant for our claims regarding the increased SATB1 aggregation in human cells in relation to the revised Fig. 6f,g,h and Supplementary Fig. 6c,d. This is also discussed in Lines 479-482, which read: “This is particularly important given the higher LLPS propensity of the human long SATB1 isoform compared to the murine SATB1 (Fig. 5d). Therefore, human cells could be more susceptible to the formation of aggregated SATB1 structures which could be associated with physiological defects.”

      **Reviewer #3 (Evidence, reproducibility and clarity):**

      Zelenka et al., focus on a T cell genome-organizing protein, SATB1, to show that SATB1 undergoes liquid liquid phase-separation (LLPS), and distinct isoforms confer different LLPS-related biophysical properties. They generate a long-isoform specific antibody and conduct several experiments to test for LLPS and compare LLPS properties between the long-isoform relative to the whole SATB1 protein population. Given that SATB1 plays important roles in T cell development and in cancer, interrogating SATB1 biophysical properties is an important question. However, there are multiple problems with the experimental setup and data that weaken their support of the conclusions. I will detail some of the major issues below:

      Regarding phase-separation There are several assays to determine whether a protein undergoes LLPS. 1. One of the first the authors address is the spherocity or roundness. Indeed, formation of spherical droplets is one evidence of the liquid nature of a protein. However, the authors use fixed preparations (which can introduce artifacts), not free-floating protein, and determine roundness by showing a 2D image. Roundness should take into account the diffraction-limits of fluorescent imaging, as many structures can be imaged to appear round by the detector. There are quantifiable measurements that can be taken on 3D images to show roundness. This would best be shown using non-fixed protein.

      • We thank this Reviewer for several insightful comments. Although, we agree with most of them, we should highlight the main goal of our manuscript, i.e. to investigate the SATB1 protein with an emphasis on its physiological roles in primary developing murine T cells. We highlight this already in the introduction in Line 64 “In this work, we utilized primary developing murine T cells,...” and mainly also in the respective part of the result section: “To probe differences in phase separation in mouse primary cells, without any intervention to SATB1 structure and expression, we first utilized 1,6-hexanediol treatment, which was previously shown to dissolve the liquid-like droplets34.(Lines 203-205)”

      • We believe that this is a very important aspect of our study that should not be overlooked. The majority of proteins perhaps behave differently under physiological and in vitro conditions. However, due to the extensive post-translational modifications affecting the properties of SATB1, its completely different localization patterns between primary developing T cells and other cell types but especially cell lines and many other aspects, it was of utmost importance to focus our research on primary T cells. Unfortunately, this was accompanied with multiple difficulties, such as that we have to use fixed cells as this is the only way to visualize SATB1 in these cells. Alternatively, one could create a new mouse line expressing a fluorescently tagged SATB1 protein, but this is beyond the scope of our work.

      • However, we should also note that many LLPS-related studies do not pay any focus on primary physiological functions of proteins and they simply focus on the investigation of protein’s artificial behavior in in vitro conditions. Having said that, we too extended our experiments in primary cells to the ex vivo studies in cell lines to further support our claims. In these experiments, we utilized live cell imaging in Fig. 4-6, quantified the spherocity in Supplementary Fig. 6, showed the ability of speckles to coalesce in Fig. 4c and also used FRAP in Fig. 4f and also in the revised version of the manuscript in Supplementary Figure 6f. Moreover, we should note that most of these experiments were designed and performed during 2017 and 2018 conforming with the standards. We are well aware of the progress in the field and impact of fixation on LLPS, as described in Irgen-Gioro et al., 2022 (https://doi.org/10.1101/2022.05.06.490956), but after over seven months of review process in another journal we also believe that these aspects should be considered not to delay further progress of the SATB1 field.

      Regarding the isoform specificity of SATB1 biophysical properties 1. The authors generate a long isoform-specific antibody. However, the western blot is not convincing that this is indeed specific to the long isoform as there is a rather large smear. Can this be improved with antibody preabsorption? Since this is a key reagent for the manuscript, improvement in antibody quality is essential.

      The custom-made antibody for the long isoform has been raised against the unique 31 amino acids long peptide present in the long SATB1 isoform. The polyclonal serum has undergone affinity chromatography utilizing the immobilized peptide (antigen) to purify the antibody. In the revised version of the manuscript we have included another immunodepletion experiment with cleaner bands (Fig. 1f). Moreover, please read our answer to Major comment #2 of Reviewer 1 that follows: • The long antibody was raised in mice inoculated with the extra peptide present in the long isoform only. Therefore, the capacity of this antibody precipitating the shorter isoforms, which do not express the sequence of the extra peptide (EP, Figure 1a) in not possible.

      • We have repeated the immunodepletion experiment and we now provide the results in Fig. 1f and Supplementary Fig. 1b. The western blot in Fig. 1f is now cleaner and supports quite convincingly the presence of a long SATB1 isoform. Given the lack of isoform-specific knockouts which we could utilize to immunoprecipitate or detect the different isoforms in a single cell (or cell population), the utilized approach of immunodepletion and subsequent western blotting is the approach we thought of implementing.

      • As shown in Fig. 1f and Supplementary Figure 1b, the long isoform SATB1 antibody has the capacity to recognize the long isoform in murine thymocyte protein extracts but not the short SATB1 isoform (please compare lane 3 in the two western blots utilizing either the antibody for the long isoform -top panel - or the antibody that detects both isoforms (lower panel).

      • We have performed Immunofluorescence experiments utilizing the antibody detecting the long SATB1 isoform in thymocytes isolated from either C57BL/6 or Satb1 cKO mice. The antibody is specific to the SATB1 protein since there is no signal in immunofluorescence experiments utilizing the knockout cells (Supplementary Figure 1c).

      • We have performed Immunofluorescence experiments utilizing thymocytes and the antibody detecting the long SATB1 or a commercially available antibody detecting all SATB1 isoforms. The pattern of SATB1 subnuclear localization is similar for both antibodies (Supplementary Figure 1e).

      • In our accompanying revised manuscript Zelenka et al., 2022 (https://doi.org/10.1101/2021.07.09.451769), we provide yet another piece of evidence, consisting of bacterially expressed short and long SATB1 protein isoforms detected by western blot using either the long isoform-specific or the non-selective all SATB1 isoforms antibodies.

      • Regarding the additional bands detected in the immunoprecipitation experiment presented in the original Supplementary Figure 1b (lane 2), it is not surprising that additional bands appear in a sample of protein extracts that is used for several hours for the immunoprecipitation experiments, while the “input” sample simply denotes protein extract that is frozen at -80oC right after the preparation of protein extracts until use. It is well-established that SATB1 is the target of proteases which might as well be active during the immunoprecipitation steps (2 consecutive immunoprecipitation steps take place). Therefore, the immunoprecipitated material cannot necessarily be a copy of the input material displaying a single protein band even if protease inhibitors are included in the buffers.

      Taken together the experiments described here we showed that the antibody raised against the extra 31 aa long peptide, present only in the long SATB1 isoform, is specific for this isoform.

      1. Fig 4 Optodroplet experiment appears to show that the N-terminus of SATB1 can undergo LLPS. The results of this assay show that SATB1 has a domain that can undergo phase-separation in isolation, but it does not show that the protein itself is a phase-separating protein. The FRAP assay methods are not provided by the authors, but this is important, as continued light activation means proteins are continuously forming aggregates, and the bleaching for FRAP should be balanced with the levels of Cry2 activation. A very good description of the methods is described in the original Optodroplet paper: https://www.sciencedirect.com/science/article/pii/S009286741631666X?via%3Dihub#sec4

      We should note that we did follow the FRAP protocol provided by the recommended study Shin et al., 2017 (https://doi.org/10.1016/j.cell.2016.11.054). Indeed, these experiments are very tricky to perform and interpret, as every cell expresses slightly different amounts of protein which is directly associated with the different speed of optoDroplet formation, and thus its propensity to aggregate upon overactivation. On the other hand, there need to be continuous activation during the FRAP experiment as the lack of activation laser would result in fast disassembly of the optoDroplets, counteracting the FRAP results. Moreover, the optoDroplets actively move around the cell in all dimensions which makes the accurate measurement of signal intensity really challenging, even with an adjusted pinhole. Therefore, we do not think that FRAP is the best approach to examine the behavior of optoDroplets.

      Either way, we have now described the detailed FRAP protocol in Lines 889-898, which read: “For the FRAP experiments, cells were first globally activated by 488 nm Argon laser illumination (alongside with DPSS 561 nm laser illumination for mCherry detection) every 2 s for 180 s to reach a desirable supersaturation depth. Immediately after termination of the activation phase, light-induced clusters were bleached with a spot of ∼1.5 μm in diameter. The scanning speed was set to 1,000 Hz, bidirectionally (0.54 s / scan) and every time a selected point was photobleached for 300 ms. Fluorescence recovery was monitored in a series of 180 images while maintaining identical activation conditions used to induce clustering. Bleach point mean values were background subtracted and corrected for fluorescence loss using the intensity values from the entire cell. The data were then normalized to mean pre-bleach intensity and fitted with exponential recovery curve in Fiji or in frapplot package in R.”

      1. Description of analyses that authors prefer not to carry out

      **Reviewer #1**:

      Can they use the all and long isoform antibodies together, then subtract the signal from long isoform to conclude about the localization of the shorth isoform ?

      We thank the Reviewer for the suggestion, though given the differential efficiency of antibodies and other limitations of imaging experiments, we do not find the suggested experiment to have a potential to improve the quality of our manuscript. However, we should note that we have performed a pixel-based colocalization experiment between the signal detected by all isoform and long isoform SATB1 antibodies. Fluorocytogram of the pixel-based colocalization, based on 3D-SIM data is provided on the left, with quantified colocalization on the right of the revised Supplementary Fig. 5a.

      3) Lack of better staining with antibody against the long and short SATB1 isoforms after treatment with 1,6 Hexanediol. 1,6 Hexanediol treatment can change many other chromatin associated proteins to which SATB1 can be bound to indirectly. This experiment can

      We do understand the controversy and difficulties of experiments using 1,6-hexanediol treatment. However, we have to note that there is no better approach available for the investigation of LLPS in our primary murine T cells. We did use alternative approaches in ex vivo experiments, utilizing cell lines to validate our hypothesis without the involvement of 1,6-hexanediol.

      **Reviewer #2**:

      1. The authors mention, '...of the different SATB1 isoforms, uncovered by the use of the two different antibodies, relied in the heterochromatin areas (zone 1), where the long isoform was less frequently...' There is no supporting figure number mentioned. The authors need to show a zone-by-zone comparison images for 'all iso' vs 'long' iso of SATB1. Just to reiterate, there is a need for a heterochromatin mark to unambiguously call out the distinction.

      We should remind that there is an inherent difficulty to accurately compare localization of short and long SATB1 isoforms in primary cells, especially due to the lack of Satb1 isoform-specific knockout mice. There is no way to detect only the short isoform in these primary cells as there are only antibodies targeting the long or all SATB1 isoforms. Therefore, we cannot set up additional experiments probing these questions.

      In line with this, in the revised version of the manuscript, we toned down our statements regarding the differential localization of the two isoforms in primary cells. We only refer to it as an indication and we support it by adding references to the relevant figures. This part now reads: “Localization of SATB1 speckles detected by antibodies targeting all SATB1 isoforms and/or only the long SATB1 isoform, revealed a significant difference in the heterochromatin areas (zone 1, Fig. 2b), where the long isoform was less frequently present (see also Fig. 2a and Fig. 3c). Although, this could indicate a potential difference in localization between the two isoforms, due to the inherent difficulty to distinguish the two based on antibody staining, we refrain to draw any conclusions. (Lines 145-150)”

      1. Fig. 6a, The authors wished to see the effect of RNA on Satb1 nuclear localization. This is not related to the main theme of the paper, thus should be moved to supplementary (true for b as well). Importantly, the experiments should be performed with total cells to show the divergence of localization (like the paper the authors referred to) instead of matrix for clarity.

      • We did not wish to see the effect of RNA on SATB1 localization. In fact, there is a long history of SATB1 research that is inherently linked with the concept of nuclear matrix, a putative nuclear structure which is highly associated with nuclear RNAs. SATB1 was described many times as a nuclear matrix protein (https://doi.org/10.1016/0092-8674(92)90432-c; https://doi.org/10.1128/mcb.14.3.1852-1860.1994; https://doi.org/10.1074/jbc.272.17.11463; https://doi.org/10.1128/mcb.17.9.5275; https://doi.org/10.1021/bi971444j; https://doi.org/10.1083/jcb.141.2.335; https://doi.org/10.1101/gad.14.5.521; https://doi.org/10.1038/ng1146).

      • Moreover, our data discussed in comments 4-7 of this Reviewer, such as i. the localization of SATB1 to the nuclear zones associated with RNA and nuclear scaffold factors (Fig. 2b, Supplementary Fig. 1c), ii. colocalization of SATB1 with actively transcribed RNAs (Fig. 2c, Fig. 3g, Supplementary Fig. 2a, Supplementary Fig. 2c), iii. including its association with nucleoli (Supplementary Fig. 3b), and also iv. its computationally predicted interaction with Xist lncRNA (Agostini et al., 2013; https://doi.org/10.1093/nar/gks968) as a notable factor of nuclear matrix, all suggest that the interaction between RNA and SATB1 is plausible and potentially relevant for its function and/or at least its subnuclear localization. It is relevant even more so, when considering numerous reports on the ability of RNA-binding, poly-Q and PrLD-containing proteins to undergo LLPS https://doi.org/10.1016/j.molcel.2015.08.018; https://doi.org/10.1042/bcj20160499; https://doi.org/10.1016/j.cell.2018.03.002; https://doi.org/10.1016/j.cell.2018.06.006; https://doi.org/10.1093/nar/gkaa681), including RNAs specifically regulating LLPS behavior, especially for poly-Q and PrLD-containing proteins, such as SATB1 (https://doi.org/10.1126/science.aar7366; https://doi.org/10.1126/science.aar7432; https://doi.org/10.1016/j.ceb.2019.03.007; https://doi.org/10.1038/s41598-020-57994-9; https://doi.org/10.1016/j.molcel.2015.09.017; https://doi.org/10.1038/s41598-019-48883-x; https://doi.org/10.1038/s41467-019-11241-6).

      • It should also be noted that SAF and various hnRNPs, as the most prominent proteins of nuclear matrix were many times reported to phase separate (https://doi.org/10.1016/j.molcel.2019.10.001; https://doi.org/10.1074/jbc.ra118.005120; https://doi.org/10.1016/j.celrep.2019.12.080; https://doi.org/10.1038/s41467-019-09902-7; https://doi.org/10.1016/j.molcel.2017.12.022; https://doi.org/10.1074/jbc.tm118.001189). All these aspects show that the relation between nuclear matrix, SATB1 and RNA are quite relevant to our manuscript.

      • Moreover, in light of the aforementioned information, we believe that it is much clearer to follow the protocol we did – i.e. to remove soluble proteins by CSK treatment and then, upon RNase treatment, extract the released proteins using ammonium sulfate. In an experiment utilizing whole cells, one would need to microinject RNase A into the nucleus, which 1. is very challenging for primary T cells having a radius of 3-5 micrometers, 2. is of low throughput, 3. would not allow for released protein removal which would thus make the results hard to interpret. Please note that in the reference paper, the authors used cell lines overexpressing heterologous GFP-tagged proteins, which is not related to our setup.

      Note: This preprint has been reviewed by subject experts for Review Commons. Content has not been altered except for formatting.

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ormatika.hu/?wptouch_switch=desktop&redirect=https%3A%2F%2Fwww.dlsoftex.com%2Fsitemap.xml9666http://www.oldresianclub.org.ar/bloques/bannerclick.php?id=19&url=https%3A%2F%2Fwww.dlsoftex.com%2Fsitemap.xml9667http://www.oldtimer.ru/bitrix/rk.php?goto=https://www.dlsoftex.com%2Fsitemap.xml/9668http://www.olondon.ru/bitrix/rk.php?goto=https://www.dlsoftex.com%2Fsitemap.xml/9669http://www.omareps.com/external.aspx?s=www.dlsoftex.com%2Fsitemap.xml9670http://www.omoqlja.bassfishing.org/OL/ol.cfm?link=https://www.dlsoftex.com%2Fsitemap.xml/9671http://www.old.ventmax.ru/bitrix/rk.php?goto=https://www.dlsoftex.com%2Fsitemap.xml/9672http://www.omsk.websender.ru/redirect.php?url=https://www.dlsoftex.com%2Fsitemap.xml/9673http://www.onfirepro.com/frame_view.php?site_url=www.dlsoftex.com%2Fsitemap.xml9674http://www.offendorf.fr/spip_cookie.php?url=https://www.dlsoftex.com%2Fsitemap.xml/9675http://www.oneillreps.com/external.aspx?s=dlsoftex.com%2Fsitemap.xml9676http://www.oncoforum.ru/bitrix/rk.php?goto=https://www.dlsoftex.com%2Fsitemap.xml/9677http://www.onlineguiden.dk/redirmediainfo.aspx?MediaDataID=45b76158-9e7e-4bef-ac42-0e39f848670f&url=https://www.dlsoftex.com/sitemap.xml9678http://www.online-proxies.com/count_hits.php?url=https://www.dlsoftex.com%2Fsitemap.xml/9679http://www.oneclick.bg/openx/www/delivery/ck.php?ct=1&oaparams=2__bannerid=275__zoneid=51__cb=1e55a56a8b__oadest=https%3A%2F%2Fwww.dlsoftex.com%2Fsitemap.xml9680http://www.omnistor.pl/trigger.php?r_link=https%3A%2F%2Fwww.dlsoftex.com%2Fsitemap.xml9681http://www.onlinegreece.gr/?lang=eng&url=https%3A%2F%2Fwww.dlsoftex.com%2Fsitemap.xml9682http://www.onzelievevrouwetoren.nl/beleefamersfoort/link.php?site=https%3A%2F%2Fwww.dlsoftex.com%2Fsitemap.xml9683http://www.only-r.com/go?https://www.dlsoftex.com%2Fsitemap.xml/9684http://www.openindex.io/outlink?ssi=4282426198a584a2&url=https://www.dlsoftex.com%2Fsitemap.xml/9685http://www.oostende.net/cgi-bin/scripts_onetpages/in_frames.cgi?https://www.dlsoftex.com%2Fsitemap.xml/9686http://www.npb.scforum.jp/jump.php?uid=991&url=https://www.dlsoftex.com%2Fsitemap.xml/9687http://www.onplanlab.com/?exit=https://www.dlsoftex.com%2Fsitemap.xml/9688http://www.oppuz.com/redirect?application=avon&track%5Baction%5D=rclk&track%5Binfo%5D%5Baction_src%5D=sm&track%5Binfo%5D%5Buser_id%5D=5bccdd5170616ef1af028384&track%5Binfo%5D%5Betag%5D=d6208572-262b-4b34-834e-abc9575159b7&url=https%3A%2F%2Fwww.dlsoftex.com%2Fsitemap.xml9689http://www.openherd.com/adredirect.aspx?adType=SiteAd&ItemID=9539&ReturnURL=https://www.dlsoftex.com%2Fsitemap.xml/9690http://www.openherd.cn/adredirect.aspx?adType=SiteAd&ItemID=9510&ReturnURL=https%3A%2F%2Fwww.dlsoftex.com%2Fsitemap.xml9691http://www.optimaze.ru/forum/go.php?https://www.dlsoftex.com%2Fsitemap.xml/9692http://www.opsoftware.com/IT/ViewSwitcher/SwitchView?mobile=True&returnUrl=https%3a%2f%2fdlsoftex.com%2Fsitemap.xml9693http://www.orchidtropics.com/mobile/trigger.php?r_link=https%3A%2F%2Fwww.dlsoftex.com%2Fsitemap.xml9694http://www.orbt.ru/bitrix/redirect.php?goto=https://www.dlsoftex.com%2Fsitemap.xml/9695http://www.orenburg.websender.ru/redirect.php?url=https://www.dlsoftex.com%2Fsitemap.xml/9696http://www.optimsklad.ru/bitrix/rk.php?goto=https://www.dlsoftex.com%2Fsitemap.xml/9697http://www.orient-explorer.net/Redirect.asp?url=www.dlsoftex.com%2Fsitemap.xml9698http://www.optina-pustin.ru/redirect.php?to=https://www.dlsoftex.com%2Fsitemap.xml/9699http://www.osaka-kaisya-setsuritsu.com/column/?wptouch_switch=desktop&redirect=https://www.dlsoftex.com%2Fsitemap.xml/9700http://www.orth-haus.com/peters_empfehlungen/jump.php?site=https://www.dlsoftex.com%2Fsitemap.xml/9701http://www.orthlib.ru/out.php?url=https://www.dlsoftex.com%2Fsitemap.xml/9702http://www.osmarmarine.com/?goto=https://www.dlsoftex.com%2Fsitemap.xml/9703http://www.osa-defence.ru/bitrix/redirect.php?goto=https://www.dlsoftex.com%2Fsitemap.xml/9704http://www.otteryantiques.co.uk/link.php?url=https://www.dlsoftex.com%2Fsitemap.xml/9705http://www.otourdumonde.fr/?wptouch_switch=desktop&redirect=https%3A%2F%2Fwww.dlsoftex.com%2Fsitemap.xml9706http://www.ottawakiosk.com/ad.php?url=https://www.dlsoftex.com%2Fsitemap.xml/9707http://www.osnovit.com/bitrix/redirect.php?goto=https://www.dlsoftex.com%2Fsitemap.xml/9708http://www.ostrov77.ru/forum/away.php?s=https://www.dlsoftex.com%2Fsitemap.xml/9709http://www.ourhouse.dk/redirect.php?action=url&goto=dlsoftex.com%2Fsitemap.xml&osCsid=qi0u37q336fdpbcao38f6mdb209710http://www.ourhometown.ca/openx/www/delivery/ck.php?ct=1%26oaparams=2__bannerid=199__zoneid=6__cb=449b026744__oadest=https://www.dlsoftex.com%2Fsitemap.xml/9711http://www.optina-pustin.info/redirect.php?to=https%3A%2F%2Fwww.dlsoftex.com%2Fsitemap.xml9712http://www.ovachat.cz/redir.php?URL=https://www.dlsoftex.com%2Fsitemap.xml/9713http://www.outrest.ru/go.php?url=dlsoftex.com%2Fsitemap.xml9714http://www.overheadgaragedoors.com/redirect.php?ul_id=248&return_url=https://www.dlsoftex.com%2Fsitemap.xml/9715http://www.office-rental.net/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      Useful Information

  8. Sep 2021
    1. Author response


      September 9, 2021

      We would like to thank ASAPbio for selecting our preprint for review! We are excited to contribute to this new process and hope others will find it as helpful as we have. The comments generated by the “crowd” were detailed and thoughtful. Below we respond to the major discussion points and if there were specific reviewer comments relevant to the discussion point, we also included that statement. We also responded to each specific comment. We would love to continue this discussion, so we invite further feedback and responses! Thanks so much for your time.

      -Chelsea Kidwell, Joey Casalini, and Minna Roh-Johnson


      Major Discussion Point #1:One of the most important claims is that mitochondria are the organelles responsible for the activation of the signals of cell proliferation. However, a previous report by the last author reported that macrophages transfer cytoplasm to recipient cells. It cannot be excluded that other organelles or cellular fragments are transferred as well and contribute to the observed effects (ERK activity). Perhaps a good way to solve this would be the use of macrophages that are devoid of mitochondria. At least, this aspect should be discussed in the manuscript.

      🡪 We had first considered two approaches to test the requirement and sufficiency of macrophage mitochondria in cancer cell proliferation. The first was to generate rho-zero macrophages (mtDNA-deficient), as you mention in your comment, such that the macrophages did not have functional mitochondria. However, we use primary human macrophages for all of our studies, and these cells would not survive long enough to generate rho-zero cells (which requires that the cells be treated with low levels of ethidium bromide for weeks). The second is to biochemically purify mitochondria from macrophages and directly inject these mitochondrial preps into breast cancer cells. We actually did this experiment, and cancer cells injected with purified mitochondrial preps exhibited higher proliferation (by live timelapse microscopy) compared to control cells. However, we also found that the mitochondrial purifications were not clean, and contained other membranous components in the cytoplasm. We tried centrifugation-centric approaches, as well as IP-ing against a mitochondrially-localized tag, but in all cases, the mitochondrial preparations contained other cytoplasmic components. Therefore, we did not feel that this approach was an adequate way to test effects of specifically the mitochondria. We certainly wanted to discuss this aspect in the manuscript, but unfortunately, we were limited due to space. If folks have suggestions on how to best purify mitochondria, we’d love to know, so please reach out.

      However, in terms of the bigger question of whether the induced proliferation in cancer cells is specifically due to ROS accumulation in transferred macrophage mitochondria, we tried to address this question with the mito-KillerRed experiments, where we generate ROS using optogenetics, and ask whether this accumulation is sufficient to induce cancer cell proliferation (which we showed it was). We also showed that this same approach could induce Erk activity, and then in separate experiments, we show that macrophage mitochondrial transfer results in accumulation of ROS and increased Erk activity. We feel that these experiments support our conclusions, however, we’d love for a way to link it all together. Unfortunately, we are not convinced that such experiments are possible at this time.

      Major Discussion Point #2: Most of the positive examples of transferred mitochondria discussed appeared in a small clump. However, there also appears to be another population that was more diffuse and co-localizes with host mitochondria (e.g., Fig2B, bottom right panels). It would be helpful to show results of these sibling mitochondria for assays performed on their clumpy siblings. If they behave differently, it would be helpful to provide some explanation.

      Specific Comment: Figure 2 Majority (57%) of donated mitochondria do not colocalize with LysoTracker signal (N=24 cells, 4 donors) - Here the paper implies that some transferred mitochondria do co-localize with lysoTracker signal. More importantly, they co-localize with host mitochondria. It raises the question of whether they signal through ROS and ERK like their clumpy siblings who are in the limelight of most figures.

      🡪Yes, you are correct. There does appear to be a diffuse population of macrophage mitochondria. The majority of these mitochondria co-localize with lysotracker, suggesting that they are being actively degraded. We can’t say that they tend to co-localize with endogenous cancer cell mitochondria, however, it’s possible that this diffuse population is comprised of both mitochondria that are being degraded and mitochondria that are fusing with the endogenous network. We do not know if this population has a different effect on cancer cell behavior because we did not follow this population (mostly because once the mitochondria are degraded or fuse with the network, we can no longer follow those mitochondria!). However, we did follow cancer cells that contained punctate macrophage mitochondria. Often times this was the only population we could observe in the cell at that time, and this is the population in which we observe accumulated ROS.

      Major Discussion Point #3:The effects that are attributed to the transferred mitochondria are highly variable (figures 1F, 3A,E) and often due to a subpopulation of samples that show a few extreme values (e.g. figures 2D, 3E, S4B, S4D). This might be expected from effects that are caused by a single mitochondria (which has a small volume) that is transferred to a complete cell. This complicates the study of the transfer process and effects and should be discussed. Also, do the authors have ideas how to improve the system, to make it more robust and easier to study the effects?

      🡪The variability in the assays likely reflects the heterogeneity within the biology - Each experiment contains macrophages derived from primary monocytes that are harvested from different human blood donors! Due to the primary nature of these cells, we do expect a range of phenotypes as each donor would have a different genetic background and the monocytes were likely exposed to different environmental stimuli. In fact, even though working on this study was a giant pain due to the variability, we felt more confident about our findings because despite the heterogeneity in the system, we still observed consistent phenotypes. Below we indicate where we took a sample set and removed “outliers”, and ran the statistical tests again. The differences were still statistically significantly different, further suggesting robustness of our findings.

      However, we are always on the lookout for ways to make the system easier to study. One way that we will follow up on is using M2-like macrophages since they transfer mitochondria at a higher rate than unstimulated macrophages.

      Major Discussion Point #4: The authors conclude that the transfer of dysfunctional mitochondria generated a signal mediated by ROS that activates cell proliferation signals. The statement that "transferred mitochondria act as a signaling source that promotes cancer cell proliferation" is too strong. There is increased ROS production from mitochondria, yes, but an experiment in which ROS are decreased would be needed to properly sustain that conclusion. The title and abstract could be changed to better reflect the data.

      Specific Comment: ‘Furthermore, treatment with an ERK inhibitor (ERKi) was sufficient to inhibit ERK activity ‘- curious as to whether antioxidant treatment would reverse any proliferative phenotypes?

      🡪We wish we could quench the ROS at macrophage mitochondria. We really tried. We used a combination of ROS quenchers (NAC, mitoTempo, Tempo) and ROS readouts (mitoSOX, CellRox, DCFDA, and the 2 biosensors used in our study: Grx and Orp1), and treated cells for various amounts of time, and no matter what we tried, we could not reliably detect reduction of ROS levels in the host network or the transferred mitochondria (without killing the cells, that is). Another issue that we faced was that any pharmacological treatment would have a global effect on the mitochondrial network in the recipient cells and therefore it would not be possible to distinguish effects from global inhibition of ROS versus specifically at the site of the transferred mitochondria, and we certainly observed cell death upon treatment of ROS quenchers because of this fact. We talked to a couple of ROS experts, and they indicated that this issue is not unique to us, although we unfortunately did not have viable solutions, so if people have ideas or suggestions, please let us know!!

      However, despite our failed attempts at quenching ROS, the comment that "transferred mitochondria act as a signaling source that promotes cancer cell proliferation" is too strong of a statement… well, we don’t entirely agree given that we do perform sufficiency experiments in which weinduce ROS and observe both proliferation and ERK signaling, so we do feel reasonably justified to provide the title that we did. However, we will continue to mull over this comment. Thanks for sharing your thoughts.

      Major Discussion Point #5:The study may benefit from more direct evidence to support its conclusion of increased proliferation after mitochondrial transfer. While the RNA-seq, flow cytometry, counting of completion of cytokinesis and dry mass measurements provided in the present study do lend some support to the proliferation hypothesis, they all seem indirect. With the biomarkers labeling the mitochondria of donor and potential recipient cells, high content imaging and tracking of cells could be used to monitor cell division. A comparison of cell division rates of transfer-positive cells and transfer-negative cells will provide a more pertinent test of whether mitochondrial transfer promotes recipient cell proliferation.

      🡪We should probably do a better job at describing the dry mass measurements (QPI, quantitative phase imaging) because we view this quantification as one of the most direct measurement to monitor cell growth/division. The approach measures the changes in dry mass as the cells prepares for cell division. So not only do we get the final readout of division (complete cytokinesis), but we also get a measure of that growth rate (the cell getting ready to divide) before cytokinesis. This is why we are so tickled to collaborate with Tom Zangle’s lab because we could finally get a direct proliferation readout in real-time. We could also use this approach to follow thousands of cells at a time, a very critical aspect since mitochondrial transfer is rare event, and therefore, we need to follow many cells to have enough statistical power to quantify the growth rates. Check out some of the Zangle lab’s other papers (PMC5866559; PMC6917840; PMC4274116), and please let us know if you disagree with us!

      Major Discussion Point #6: The authors have used such a tracking-based approach on a very small scale (n=5) to measure daughter cell growth rate. However, the data do not show a statistically significant difference between the growth rates of daughters that inherited transferred mitochondria and those who did not (Fig S3). Increasing the case number via high content imaging would help obtain sufficient data points for a reliable statistical test. In addition, as suggested above, an accounting of the daughter cells' division rate for transfer positive and negative cells would provide another line of evidence to either prove or disprove the increased proliferation rate hypothesis. The same suggestion goes to the optically induced ERK activation experiments shown in Fig3F. It is also helpful to include references that studied how ERK signaling promotes proliferation and compare the evidence here with evidence or assays used in those studies as a benchmark.

      Specific Comment:Figure S3 - There is no statistical test to check for ‘increase in their rate of change of dry mass over time versus sister cells that did not inherit macrophage mitochondria’. What are the colours indicative of in S3B? Can this be reported in the figure legend.

      🡪You are right – the tracking-based approach on daughter cells is based on a small ‘n’. However, the tracking itself is performed on 1000s of cells. It’s just that in order to capture daughter cell data, we have to find a cancer cell with macrophage mitochondria (which is only ~1% of the population), and then follow that cell until it divides, and then follow BOTH daughter cells. So, even with the 1000s of cells that we followed, we could only capture a small number of daughter cells. The colors in S3B represent each individual triads – parent and 2 daughters. We will make this info clearer in the legend.

      In terms of the optically-induced ERK activation experiments, yes, it would be great to have a higher sampling. These experiments were performed at 63x so we could reliably draw small ROIs to mimic the size of a macrophage mitochondria. While we switched to lower magnification to follow cell division, we still were limited to only a few cells for the actual photoactivation. The technical aspects of this experiment were the reason for the low sampling. Despite these limitations though, we still observed increased cell division upon mito-killerred photoactivation, which we were honestly pretty surprised (and stoked) about.

      Other specific comments:

      -Figure S1A - The authors could perhaps use a more aggressive gating strategy here, clipping closer to the 231 population described in Fig S1A - picking only the center of the cluster in the upper left of the RFP vs CD11b plot would likely not affect results but make them more convincing by unequivocally excluding macrophages.

      -Figure 1D - Not sure about the 0.2% baseline assigned for the monoculture of cancer cells (that does not have the macrophages with the Emerald mitochondria). It is determined with cytometry - I am no expert on that topic, so maybe I missed something - but it looks weird to see some cells with transfer when there is a monoculture.

      🡪Due to the variable nature of the mito-mEm signal in the recipient cancer cells (i.e. transfer of one mitochondrion vs transfer of three), we found that an overlap of 0.2% set on a fully stained monoculture control was the most accurate way to gate for the recipient cancer cells. The final gating strategies used in our study were determined by FACS-isolating populations of interest based on several different gating strategies, and directly visualizing cancer cells with macrophage mitochondria without capturing macrophages or cancer cell/macrophage fusions (which is cool, but not what we wanted). To further clarify, there is no transfer occurring in the monoculture – the overlap of mEmerald signal into the transfer gate in that control sample is likely reflective of normally occurring autofluorescence. This is a very important point, so we will make this aspect clearer in the Methods section.

      -Figure S1B - Could perhaps be an interesting follow-up question for future works re: differences between cell lines and propensities to transfer mitochondria. Did the authors attempt to use other cell lines (ie, MDCK, HeLa, iPSCs, etc)?

      🡪Great question and something that we have also been thinking about. To date the only recipient cells we have used are 231, MCF10A, and PDxO cells. This would be a great avenue for future studies.

      -Figure S1B - Did the authors see an increase in growth rate in MCF10A line despite the lower growth rate?

      🡪We have not measured the growth rate in MCF10a recipient cells but something that would be great to follow up on in future studies.

      -‘physically separated from macrophages by a 0.4μM trans-well insert’ - should this read 0.4 micrometer?

      🡪Yes, great catch.

      -Figure S1F - The authors wrote that they used a two-way ANOVA analysis, could you report the factors used for that analysis in the Figure legend.

      🡪Noted!

      -Figure 1B - It is difficult to see the arrowheads in 1B, suggest moving them so they are not covering the magenta fluorescence, have them point from a different angle, and make them more brightly colored. Insets here would help the reader. A negative control image from a monoculture would also be helpful, to ensure the GFP signal is not an artifact of culture conditions.

      🡪Thank you for your feedback – we will take note of this.

      -Figure 1F - For graphs that do not show zero (as in 1F), the bar should be omitted. In these cases the length of the bar does not reflect the average of the data (as it does in 1D).

      -Figure 3C - Please omit bar, see comment on panel 1F.

      🡪 In the case of Fig 1F, we modified the y-axis to eliminate empty space. The bar is representative of mean of the data displayed in both 1D as well as 1F, but we can add a broken y-axis to help make this point.

      -Figure 1 - Given that these data are fractions of a population (ie. can be described via a contingency table), isn't something like a Fisher's exact test a better measure of significance here?

      🡪We think you are referring to Figure 1D? If so, we thought that we could not use Fisher’s exact test because that test assumed parametric distributions (which we do not observe). We have been working with a biostatistician for our statistics, but please do let us know if we have it wrong.

      -Single cell RNA- sequencing - In the methods section the authors mention doing a differential analysis between the cells that received the mitochondria and the cells that didn’t. It might be worth introducing a figure (a heatmap or a U-MAP) relating to this analysis. Single cell sequencing would not only affirm the heterogeneity between these two populations but also help in highlighting the novel cell surface markers associated with the two populations.

      🡪Yeah, good point – we can add a UMAP.

      -‘mito-mEm+ mitochondria remained distinct from the recipient host mitochondrial network, with no detectable loss of the fluorescent signal for over 15 hours’- It is surprising that the transferred mitochondria do (or cannot) fuse with the host 231 mitochondria.

      🡪We were also initially surprised to find that the transferred mitochondria do not fuse with the host 231 network! We think that the lack of fusion is due to the fact that the transferred mitochondria do not exhibit membrane potential (which is required for mitochondrial fusion). We also think that these results open interesting lines of questioning: Why are these depolarized mitochondria not degraded? Is this an active avoidance of the mitophagy pathway? How dynamic are these punctae? Many fun and interesting questions regarding the long-lived nature of these transferred mitochondria.

      -It is unclear in these images, but the 231 mitochondria appear fragmented too. Is it possible that the mitochondrial fusion machinery (Opa1 or Mfn1/2) are inactive?

      🡪231 cells are capable of fission and fusion (PMC7275541, PMC3911914, and in our own timelapse recordings), so we think that the machinery is functional. However, we don’t know whether the 231 mitochondrial machinery changes after receipt of macrophage mitochondria. Interestingly, the references above both investigate how mitochondrial dynamics promote tumor metastasis. A fascinating future direction could include an investigation to how macrophage mitochondrial transfer influences tumor cell mitochondrial dynamics.

      -Figure 2B - What does the MTDR staining of the macrophage mitochondria prior to transfer look like? Important to check this to confirm that only the transferred mitochondria had lower membrane potential.

      -‘significantly higher ratios of oxidized:reduced protein were associated with the transferred mitochondria versus the host network’-Here too, it would be important to check the mito-Grx1-roGFP2 readout of macrophage mitochondria prior to transfer.

      🡪The way that these comments are written is as if we already know that the mitochondria are dysfunctionalbefore transfer to cancer cells. But we actually do not know if that is the case. It’s also possible that macrophage mitochondria become dysfunctional once they are in the cancer cell, which would be equally cool. So, we are actively investigating this biology.

      -Figure 2A, 2BB and S1D - How were the colocalizations assessed? Was it just a visual assessment? Given the importance of these experiments for the whole story, having a quantification of the level of colocalization with each dye would be important.

      🡪This is a good point and it should be straightforward to include a Pearsons coefficient for these markers.

      -Figure S1D - The paper makes an argument about mitochondria transferred from Macrophages (marked green) having positive DNA stain (gray), but appearing depolarized (negative TMRM stain). The image in FigS1D is peculiar, as the majority of the 231 cells' mitochondria appear to not have any DNA stain but maintain membrane potential (positive in TMRM), while some (just above the green macrophage mitochondria) do have both DNA stain and membrane potential. The authors might want to clarify whether this is a typical scenario, and if so perhaps offer an explanation as to why the 231 mitochondria exhibit such heterogeneity.

      🡪The images in S1D are of a single z-plane image therefore the DNA signal in the endogenous network is more readily visible in planes that are not shown.

      -‘we confirmed that 91% of transferred mitochondria were not encapsulated by a membranous structure, thus excluding sequestration as a mechanism for explaining the lack of degradation or interaction with the endogenous mitochondrial network’ - This is based on co-staining with MemBrite 640/660, which is a dye that "covalently labels the surface of live cells", thus there is a concern as to whether this approach allows to study whether the mitochondrium is encapsulated by an endomembrane.

      🡪Thank you for your feedback. We actually do think that Membrite can label endomembrane in addition to the plasma membrane. This is from the published Membrite protocol: “MemBrite™ Fix dyes are designed to be fixed shortly after staining, when they primarily localize to the plasma membrane/cell surface. Cells also can be returned to growth medium and cultured after staining, however, dye localization in live cells changes over time. Labeled membranes become internalized, so staining gradually changes from cell surface to intracellular vesicles, usually becoming mostly intracellular after about 24 hours. Internalized MemBrite™ Fix dye is usually detectable for up to 48 hours after staining, though this may vary by cell type”.

      In our hands, we found that the dye started to become internalized and labeled vesicles within the cell within a few hours of staining. The images in the panels that you refer to came from time-lapse imaging experiments of between 10-15 hours, therefore the cells have internalized the MemBrite signal allowing for the visualization of internal vesicles. Also, in other studies not in the preprint, we perfused purified mitochondrial preparations onto 231 cells. The 231 cells took up the mitochondria from the environment, and all of these engulfed mitochondria were surrounded by a MemBrite positive membrane! These results further suggest that if the transferred mitochondria were encapsulated by a membrane, we would be able to visualize it.

      _-‘macrophage mitochondria are depolarized but remain in the recipient cancer cell’ -_Did the authors examine the extent of cancer cell death in their co-culture system (due to the activation of apoptosis by the depolarized mitochondria)?

      🡪We do not find any evidence of abnormal levels of cell death by both flow cytometry assays as well through our QPI image analysis.

      -Figure 2C–D - Like in Fig 2B, in the bottom left of panel of Fig 2C there are a lot of donor mitochondria not in highly oxidized state and the growth/proliferation phenotypes apply mostly to donor mitochondria that appear 'clumpy'.

      -Perhaps it is worth commenting on whether there is a link between donor mitochondrial morphology and the suspected proliferation-enhancing phenotype.

      🡪The images in Fig. 2C are of the same cell – a single recipient cancer cell which is expressing the Grx biosensor. The donor mitochondria are labeled with an arrowhead, the rest of the yellow/green signal (bottom right) is from the endogenous host network and therefore we do not expect it to be in a highly oxidized state (ie. more yellow than green).

      Regarding the mito morphology and proliferation – great question, and one that we are actively working on!

      -‘At 24 hours, we observed a similar trend, but no statistically significant difference (Fig. S4D). These results indicate ROS accumulates at the site of transferred mitochondria in recipient cancer cells’ - if a specific sensor fails to show a significant oxidation at 24 hours compared mito-Grx1-roGFP2 which reports on mitochondrial glutathione redox state, does that mean there are ROS independent ways to oxidize Glutathione? The authors did see cell growth phenotype both in 24 and 48 hours which suggests that something is happening in 24 hours despite no significant difference in ROS H2O2 sensor.

      🡪The additional biosensor that we used – mito-Orp1-roGFP2 - has been engineered to be a readout of one type of ROS – H2O2. The Grx probe is a surrogate for ROS of any type, of which there are many! To us, it is not completely unexpected that they would behave differently over time since they are readout for two separate things, and it generates an interesting possibility that different types of ROS accumulate over time. Given that the Grx probe shows an increase at 24 hours, which is when we observe the proliferation phenotype, we think we are on the right track. If you have ideas on robust ways to directly observe specific types of ROS, we would love to know!

      -The differences in ratio for the two sensors used are not very convincing. In Fig 2D and Fig S4B and D the “host” and “transfer” populations are very similar. The difference seems only due to the presence of a few outliers in the “transfer” populations. More importantly, sometimes it seems that these outliers come mostly from one donor rather than being present in all 3 donors. It could be good to show histograms of the two populations for each replicate/donor and maybe redo the stats excluding these outliers.

      🡪We think that the heterogeneity that is observed is due to the biology in the system – we are using primary macrophages derived from blood donors. However, for the data represented in Fig 2D, just as a test case, we took out the top four “outliers” in that data set and re-ran the Wilcoxon matched-pairs signed rank test and the p-value was 0.0010 (***), further suggesting that the ROS biosensors are revealing consistent and robust results.

      -Figure S5C - it seems like the percentage of cells that divided is the same for unstimulated cells and cells with stimulated mito-KillerRed. Isn't this contrary to the expectation? The figure shows that photobleaching cytoplasm decreased % cell division, which is puzzling.

      🡪The mean percent of cells that divided in unstimulated and mito bleach are very similar and was not significantly different. One point to be made that may not be well illustrated in our graphical representation is that if you look at the matched data (points connected are averaged per FOV for each condition in the same experiment) the trend shows that the mito bleach does seem to have an increase in cell division which is washed out with the average bar overlay. We should note that this experiment is very “noisy” and therefore we needed a lot of N to be able to detect significant changes. We are currently thinking about other ways to demonstrate sufficiency as it relates to cell proliferation – any experimental suggestions would be very welcome! Thanks for the feedback.

      -Figure 3A - In the 'cyto' condition 6 out of 13 fields have no cells that divide. Is that expected? What is the percentage of dividing cells for cells that were not illuminated at all (a control that is lacking)? There is large variation, ranging from 0% to 22%. The evidence that illumination of KillerRed leads to increased proliferation is rather weak. Also, since Cyto and Mito are different cells, is a "paired" statistical test the right kind of test to use here?

      🡪Additional data pertaining to Fig. 3A can be found in Fig. S5C, which includes the control for cells not illuminated at all. Having no cells that divide in a field of view is not surprising to us – the doubling time for these cells is ~35 hours, and we imaged for 18 hours. Also, for each field of view, our ‘n’ for each field of view was often 6-8 cells because we performed these experiments at 63X to allow for accurately drawn regions of interest for photoactivation. We also internally controlled every experiment (each experiment consisted of fields of view that had either mito activation, cyto activation, or no-activation controls, all of which were imaged overnight with multiple x/y positions). Cells that left the field of view over the 18 hours of imaging could not be quantified. It’s this sampling that caused the large variation in the graph. But again, as with many of our experiments, despite this variability, we still observe a significant difference in our experimental conditions over control cyto bleach. As for the statistical test, our understanding is that given each experiment is internally controlled, and we compare within each experiment, a paired statistical test is appropriate here. We will consult with our biostatistician to confirm, though.

      -‘ROS induces several downstream signaling pathways’ - We would not expect the authors to investigate every signaling pathway, but wonder if the PI3K pathway was explored? It seems to be the other major cancer/proliferative pathway induced by ROS.

      🡪Yes, this is a very good point! We actually assessed three different pathways at first – ERK, PI3K-AKT, and NLRP3/inflammasome. While analyzing these 3 pathways simultaneously, we discovered that ERK inhibitors resulted in decreased proliferation in cancer cells with macrophage mitochondria. As a result, we then focused on the ERK pathway. We still do not know if PI3K-AKT or NLRP3/inflammasome pathways play a role in this biology because we have not gone back and revisited these experiments yet, however in figure 3F, ERKi treated recipient cells exhibit a partial ‘rescue’ of baseline proliferation. This suggests that other pathways may indeed be involved and we plan to investigate this possibility.

      -‘Recipient 231 cells had significantly higher cytoplasmic to nuclear (C/N) ERK-KTR ratios compared to cells that did not receive transfer’-Since two different quantification styles with opposite fraction values were used, is it possible to please specify which one was used here.

      🡪Will do!

      -Figure 3B - Please show the outlines of the nuclei and that of the cell.

      🡪That would be helpful, wouldn’t it? Will do!

      -Figure 3D - it is peculiar that ERK-KTR in Fig 3D is so strongly cytosolic while in Fig 3B it is almost exclusively nuclear. If this sensor behaves differently in different situations, the authors may want to comment on how that would affect their conclusions.

      🡪The panels in Fig. 3B were taken with the ImageStream flow cytometer which takes a lower resolution image of a single plane of a cell in suspension in the flow stream. In Fig. 3D, those images are from confocal spinning disk microscopy which allows for higher resolution, z-stack images of adherent cells on glass. Therefore, we think the differences that you point out are likely due to the fact that the two images come from very different imaging systems.

      -Figure 3E - The effect of 'opto-induced' ERK activity is weak. The initial ERK-KTR is 1 at time point zero (as the data is normalized to this timepoint) and around 1 for both the cyto and mito condition. A statistical difference is observed, but the effect is minor and it is unclear whether it is biologically meaningful. The 'cyto' condition shows an average below 1 and the mito condition remains 1, suggesting that ERK activity remains constant when ROS are produced in the mitochondria.

      -Also from S8C and 3E it appears cyto actually shows a decrease rather than mito showing an increase, could the authors comment on this?

      🡪We have a few thoughts on this. The first is that we don’t expect a dramatic change in ERK signaling because the ROS accumulation is localized to a small region in the recipient cell. This is not a situation where we would expect a large-scale change because we are adding a growth factor. We can understand that the change in ERK activity may appear to be minor, but our data suggest that these subtle changes in kinase signaling translate into significant changes in downstream behavior – proliferation. The way that we interpret differences as “biological meaningful” is whether they exhibit a functional response, and in our study, we show that inhibiting the induction of ERK activity in cancer cells with macrophage mitos inhibits proliferation. What is most interesting to us is that cancer cells that do not have macrophage mitochondria have an unchanged fraction of cells in G2/M phase of the cell cycle in response to the concentration of ERK inhibitor we used, suggesting that the ERK inhibition specifically blocks macrophage mitochondria-induced proliferation.

      In Fig. S8C, bleaching a region of cytoplasm does seem to cause a decrease in ERK activity over time. We really can’t explain this result. However, we do think that ERK activity is higher in mito-bleached cells because mt-ROS is generating an increase in ERK activity which compensates for the decrease in activity that occurs when the cytoplasmic region of interest is photobleached. It’s still a head scratcher, though, but we did perform internal controls for every experiment (as we describe above), and the mito-bleach, cyto-bleach, and no-bleach conditions were run side-by-side such that we can make apples-to-apples comparisons.

      -‘patient-derived xenografts (PDxOs)’ - As a control it would be relevant to include a normal mammary organoid model perhaps from the same patient to demonstrate that the transfer of mitochondria specifically to the cancer cells is more beneficial.

      🡪Using a normal mammary organoid cells as a control to compare efficiency of transfer and downstream phenotypes would be very interesting. Due to the fact that these are patient-derived organoids, we are unable to acquire non-malignant cells from the same patient. Expanding our studies in the MCF10A cell line that we utilized in this paper would be an alternative to what you propose and would also expand our understanding of general biology underlying mitochondrial transfer.

      -‘macrophages to both HCI-037 and HCI-038 PDxO cells (Fig. 4G)’ - Why is M0 able to transfer efficiently to HCL-037 tumour when its mitochondrial network is less fragmented as M2?

      🡪These results really stood out to us. It was quite surprising that in HCI-037, both M0 and M2 macrophages were able to transfer their mitochondria at similar efficiencies, but in HCI-038, M2 macrophages were more efficient at transfer. HCI-037 is a primary tumor, and HCI-038 is a metastases from the same patient, so there are some exciting avenues of study to examine how macrophage mitochondria transfer differs at the primary versus metastatic site. There is still very little known about how donor cell dynamics influence mitochondrial transfer!

      -Are mito transfer from M0 depolarised and accumulate ROS or show increased ERK activity or increased cell proliferation?

      🡪Yes – all studies, except studies pertinent to fig 4 (where we assessed macrophage differentiation states), were done with M0 macrophages.

      -‘M2-like macrophages preferentially transferred mitochondria to the bone metastasis PDxO cells (HCI-038) when compared to primary breast tumor PDxO cells (HCI-037)’ -The authors may want to check this statement here as it is in consistent with their data plot. In Fig. 4G, M2/PDxO transfer percentages for HCI-037 and HCI-038 are about the same, unless the authors provide statistical tests to prove otherwise. Instead, M0 appears to transfer mitochondria to HCI-037 much more efficiently than it does HCI-038.

      🡪Upon re-reading our sentence again, we now realize that it’s actually quite poorly written, so we can understand the confusion! What we meant to articulate is that M2-like macrophages are better at transferring mitochondria to HCI-038 than M0 macrophages. Whereas in HCI-037, we do not observe the same preferential transfer (ie. M0 and M2 can transfer at the same efficiency). We will certainly clarify this language in the manuscript.

      -‘M2-like macrophages exhibit mitochondrial fragmentation’ - Is there a correlation between the status of the mitochondrial network in the donor and the % of transfer to the recipient? If so, this would be a correlation that would support the conclusions.

      🡪Yes, please see Fig. 4C for transfer rates with different donor subtypes and Fig. 4H for a general working model on how we think these data fit into the larger picture.

      -‘accumulate ROS, leading to increased ERK activity’ - Did the authors obtain similar results with the PDXOs? It would be an interesting observation if the primary samples also exhibit a mechanism similar to established cell lines wherein there are more accumulated genetic changes.

      🡪Our main limitation with PDxOs is overcoming the technical hurdles related to our downstream assays. These include introducing relevant reporters and generating stable lines in the PDxOs, and imaging at high-resolution when the PDxOs are cultured in 3D. However, we are very interested in this question as well, and are actively thinking about ways to overcome these hurdles.

      -It would also be interesting to examine whether there is any difference in the ROS-ERK mechanism for primary and metastatic tumour.

      🡪We agree and this is an active avenue of investigation for us. We agree and are currently pursing models to understand how our findings fit into the larger picture of tumorigenesis and metastatic potential. We had spent months pursuing anin vivo approach using a murine Cre/LoxP system to genetically label mouse macrophage mitochondria with GFP. We crossed mice which express Cre under a monocyte-specific promoter (Jax, SN: 004781) and mice with germline expression of Lox-Stop-Lox-3xHA-EGFP-OMP25 (Jax, SN: 032290) with the expectation of seeing Cre-based excision of the stop cassette – thus resulting in offspring with macrophages expressing mitochondrial-localized GFP. However, the macrophages of the resulting offspring do not express GFP (by flow cytometry, imaging, and western blot analysis), despite the PCR-verified presence of both transgenes and the excision of the stop cassette. Needless to say, this was quite frustrating! We are currently in the process of developing a newly available MitoTag model which has been optimized for visualization purposes (Jax, SN: 032675). If you have any suggestions or advice on this matter we would much appreciate your thoughts!

      -‘in cancer cells that receive exogenous mitochondria’ - Since these macrophages also transfer mitochondria to non-malignant cells, such as MCF10A cells shown in Fig S1B, perhaps the authors could comment on whether this is part of a physiological process that would also promote normal cell growth?

      🡪 There are so many questions regarding when and why macrophages might transfer mitochondria. In general, mitochondrial transfer is observed in stressed cells. Our data suggest that transfer happens to MCF10A cells although at a much lower rate than their malignant counterparts, 231 cells, but we do not know whether similar downstream mechanisms and phenotypes are also occurring in the non-malignant cells. Thanks for your feedback – more to come here!

  9. Jul 2021
    1. Note: This rebuttal was posted by the corresponding author to Review Commons. Content has not been altered except for formatting.

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      Reply to the reviewers

      Dear reviewers,

      We thank all reviewers for and their appreciation of our work and even more so for their constructive comments and suggestions, which will significantly improve the quality of the manuscript. We were able to complete the revision and address all reviewer comments. Aside a more stringent discussion of the literature, and rewording of certain paragraphs for clarity, we also generated additional experimental data.

      More importantly, to address the concern that we did not provide a positive marker for the intranuclear compartment, we present new images. We attempted to label gamma-Tubulin by generating new antibodies, GFP-tagged strains, and trying multiple commercial antibodies since the beginning of the project. Only recently we found an antibody providing a more specific signal at the expected location, although with some likely cross-reactivity with alpha- and beta-tubulin, and now show these data in the supplements. Additionally, we generated expansion microscopy samples stained with a fluorophore-coupled NHS-Ester, a bulk protein label. These data show that the centrosome contains an exceptionally protein dense hourglass-shaped region, which spans from the extranuclear to the intranuclear compartment, as revealed by centrin and tubulin co-staining. This fortifies our claims about the distinct nature of the intranuclear centrosome compartment containing the microtubule nucleation sites.

      Further, we add images of 5-SiR-Hoechst, SPY555-Tubulin, Centrin1-GFP triple labelling live cells to demonstrate the specificity of the microtubule dye and to underline that we are indeed acquiring the dynamics from the first nuclear division on.

      In terms of formatting we added line numbers and uploaded high quality figures separately. Due to the added data and panels we needed to split Fig. 1 into two separate figures, rewrote the figure legends and moved them to the end of the document.

      Please find below a point-by-point response to the comments.

      Best regards,

      Julien Guizetti

      Reviewer #1 (Evidence, reproducibility and clarity (Required)):

      The manuscript by Simon and collaborators addresses the dynamic changes of spindle and hemi-spindle microtubules occurring along schizogony in Plasmodium falciparum. The work explores the temporal correlation of the changes observed in intranuclear spindles with changes at the level of the centriolar plaque; the nuclear microtubule organizing center of these parasites, using centrin as a bona fide marker of the structure. The study shows that spindle microtubules organize from an intranuclear region, devoid of chromatin, distinct from the centrin region which had not been observed or described before. It further shows that centrin does not localize at the nuclear envelope, but it is actually extranuclear.

      This work significantly expands on previous knowledge regarding the functional and spatial organization of the nucleus in P. falciparum, and the structure once defined as "an electron dense mass on the nuclear envelope." It uses state of the art microscopy approaches such as STED, UExM and CLEM, in combination with immunolabeling, dyes and parasites over expressing fluorescent protein fusions, to address these questions.

      **Major comments:**

      • Are the key conclusions convincing?

      I find the manuscript successfully addresses the posed questions. The data presented supports the conclusions.

      • Should the authors qualify some of their claims as preliminary or speculative, or remove them altogether?

      • Would additional experiments be essential to support the claims of the paper? Request additional experiments only where necessary for the paper as it is, and do not ask authors to open new lines of experimentation.

      No

      • Are the suggested experiments realistic in terms of time and resources? It would help if you could add an estimated cost and time investment for substantial experiments.

      N/A

      • Are the data and the methods presented in such a way that they can be reproduced?

      Yes

      • Are the experiments adequately replicated and statistical analysis adequate?

      Yes

      **Minor comments:**

      • Specific experimental issues that are easily addressable.

      On the data shown in Figure 1, it is unclear to me what elements are taken into account to define "anaphase." Anaphase could be defined by using chromatin markers - such as CenH3- which have been identified in Plasmodium and the authors make use of in Figure 1F.

      We acknowledge that the term anaphase is ill-defined here. Further it suggests a mitotic morphology analogous to the one observed in “classical” models (prophase, metaphase, anaphase,…), which is not fully appropriate. In line with the comments by Reviewer 3 we, therefore, decided to use the term “extended spindle” instead (Fig. 1 & 2). This better reflects the morphological criterion on which we based the stage definition.

      • Are prior studies referenced appropriately?

      The authors state that "with the exception of centrins and gamma tubulins" few canonical centrosome components are conserved in Plasmodium. These parasites are in fact able to assemble a more or less canonical centriole for microgamete basal body formation. Widely conserved centriolar components such as Sas6 are coded by the malaria genome, and have been characterized previously. This work is neither referenced nor discussed in the manuscript.

      The reviewer is right to point out this omission. We were too much focussed on the blood stage centriolar plaques while writing this section, where centrioles are not observed. Of course centriole-like structures are relevant in other life cycle stages, such as microgametes, and should be discussed (line 104). Some previous attempts to endogenously tag Sas6 to verify its localization in blood stages were unfortunately not successful.

      • Are the text and figures clear and accurate?

      I find the timings shown in Figure 1A, with respect to the schematic quantification shown in Figure 1B, confusing. Shown as it is, one naturally correlates the images on Fig1A above with the cell cycle progression timing shown on Fig1B, below. However, by time 260min, for example, two somewhat adjacent centrin signals can be observed. Though this is defined as anaphase- by an unspecified criterium- this could very well be representative of metaphase. Nonetheless, the timing shown on Figure 1B for "anaphase" onset is 170min, which is inconsistent with the images above. I suggest that either, the quantification is shown in a different format (ex. bar plots) which could then better reflect the cell to cell variations observed (by use of error bars, for example) or that the figure explanation in the results section clarifies this issue.

      We understand how this representation is misleading and have adjusted the figure and text accordingly. We modified the time stamps in Fig. 1A (now Fig. 1C) to the scale used in Fig. 1B (now Fig. 1D) i.e. collapse of the hemispindle is t=0 and explain this in the text (line 158). Since we feel that Fig. 1B (now Fig. 1D) is a good and compact visual representation of progression through the first division we kept the bar plots in the supplements (Fig. S1), but added a title clarifying that average duration between multiple movies are shown.

      As presented, the data in Figure 1C is rather uninformative. A pattern could be more immediately extracted if dots corresponding to subsequent appearance of centrin dots in the same nucleus were connected to each other.

      Concerning the appearance of the centrin signals we adopted the good suggestion by the reviewer and connected “paired” centrin signals by lines (Fig. 1E).

      • Do you have suggestions that would help the authors improve the presentation of their data and conclusions?

      There are a number of edits required on the text. Row numbers would have been helpful in pointing these out. I point some edits below, but thorough revision of the manuscript for grammatical and synthetic errors would be beneficial.

      • Cytokinetic segmeter - please replace with "segmented"

      • Please refer to Figure 1D when appropriate - there is quite an extensive paragraph describing the results shown on this figure, but it is only referenced at the start.

      • "..., as did the and the number of branches per nucleus,..." please rewrite as appropriate.

      We apologize for not providing line numbers, but have corrected the addressed points and applied a grammatical check throughout the manuscript. We have added additional references to Figure 1D (now Fig. 2A) in the text.

      Reviewer #1 (Significance (Required)):

      This manuscript could be interested to a wide audience interested in cell cycle, cell division, cell organization and organelle positioning, infectious diseases and microscopy. However, the introduction assumes that readers are somewhat experts in the malaria field. I suggest the authors include a brief introduction of the malaria life cycle, and a schematic representation of the division mode. This will help non-experts follow the narrative more easily.

      We are happy to read that the reviewer sees value of this study for a broader audience. Following the suggestion, we added a small schematic (Fig. 1A, lines 54, 62) highlighting the relevant steps of schizogony and expanded the introduction of the life cycle (line 46).

      This work rectifies long-standing inconsistencies observed by different experimental approaches in the nuclear organization of malaria parasites during schizogony. However, what the functional consequences of the alternative modes of spindle organization in malaria could be, are not clearly stated or discussed. In this respect, as it stands, the manuscript is rather descriptive and lacks mechanistic insight. Nonetheless, the data presented are of superb quality, and the manuscript represents a tremendous leap in structural insight and imaging resolution for the field of malaria. I find the data is suitable for publication albeit minor adjustments are made (specially to Figure 1 and/or the description of the results shown in Figure 1, for consistency).

      We agree that the value of this manuscript lies in the clarification of conflicting data, unprecedented structural insight, and providing a useful working model for the malaria parasite centrosome. Although this study is ultimately descriptive it forms the indispensable basis to generate more meaningful functional insight about centrosome biology and nuclear division. Some of the functional consequences worth considering are: i) The (at least) bipartite composition indicating that centrosome functionality is spatially spread throughout the nucleoplasm/cytoplasm boundary. ii) The delayed appearance of the centrin signal after tubulin signal allows the prediction that centrosome assembly is a staged process occurring over an elongated period of time. iii) The generally amorphous structure of the compartment predicts the involvement of yet to be uncovered matrix-like proteins harbouring microtubule nucleation sites. iv) Lastly, our model has important implications for the mechanism of centrosome duplication. In a centrosome containing centrioles (like in vertebrates), the duplication event can easily be explained by physical separation of the daughter and mother centrioles. Spindle pole body duplication in yeasts is achieved by de novo formation of a new one, which remains connected by a half bridge until it is split. The centriolar plaque organization revealed here suggests that we need an entirely new model of centrosome duplication (or splitting) to describe and understand this process in malaria parasites. We now address those points more explicitly in the discussion section (e.g. lines 375, 443, 467).

      **Referee Cross-commenting**

      I agree with all the other reviewer's comments. I'm glad the reviewers seem to be experts in the field of malaria cell division and have pointed out previous studies which were not appropriately referenced. I second those comments.


      Reviewer #2 (Evidence, reproducibility and clarity (Required)):

      **Summary:**

      The manuscript by Simon et al have used advance cell biology technology like STED, expansion and live cell imaging to decipher the configuration of microtubules, centrin and nuclear pore during unconventional cell division process in malaria parasite. They have shown the dynamics of centrin and its localisation with respect to centriolar plaque that is characteristic of these parasite cell during schizogony> They also implicate from their studies that there is extended intranuclear compartment which is devoid of chromatin

      **Major Comments**

      • Are the key conclusions convincing? Yes to some extent

      • Should the authors qualify some of their claims as preliminary or speculative, or remove them altogether?

      *Some part are preliminary and speculative as there is no solid data supporting it. Please see below

      • Would additional experiments be essential to support the claims of the paper? Request additional experiments only where necessary for the paper as it is, and do not ask authors to open new lines of experimentation.

      *Yes to substantiate their claim

      • Are the suggested experiments realistic in terms of time and resources? It would help if you could add an estimated cost and time investment for substantial experiments.

      *They can do these quite quickly less than a month

      • Are the data and the methods presented in such a way that they can be reproduced?

      *Yes

      • Are the experiments adequately replicated and statistical analysis adequate?

      *Yes

      The authors present beautiful imaging and some in depth structure using tomography and CLEM to show the location of centrin which is generally considered the marker for centrosome or Microtubule organising centre in malaria parasite. These approaches are still not been applied in Plasmodium and hence very informative. Though they present some advance microscopy but a lot of these concept for hemispindle were shown earlier in many light and super resolution microscopy studies. Authors claim that they are first to show that there is space between centrin and nucleus but it has been show previously in centrin studies in Plasmodium berghei using super resolution microscopy (Roques et al 2019 Fig1 and supplementary videos1&2) as well as expansion microscopy recently by group of Brochet etal 2021.

      We thank the reviewer for the appreciation of our work. We are, indeed, not the first to describe the gap between centrin and tubulin or the nucleus. We just aimed to reiterate this finding, also visible in our data, in order to transition to the analysis of nuclear pore positioning to clarify whether centrin is actually extranuclear. Nevertheless, we should have cited the Roques and Bertiaux et al. studies again in this context, which we have now rectified (line 252).

      In addition the microtubule dynamics was also recently shown with Kinesin5 live cell imaging for schizogony in Plasmodium berghei (PMID: 33154955) which author have omitted in their manuscript.

      We thank the reviewer for pointing out the Kinesin-5 study by Zeeshan et al., which we failed to cite and discuss. We now state the findings of this publication and put it into the context of our work (see also answer to next point). Microtubule associated proteins, such as the microtubule plus end tracking EB1 and the aforementioned Kinesin-5, are indeed useful markers to investigate microtubule dynamics leading to the interesting results shown by Zeeshan et al. Nevertheless, we want to point out that labelling microtubule associated proteins (MAPs) remains an approximation of the underlying microtubule organization. As the authors in Zeeshan et al. indicate by themselves, Kinesin-5 does not decorate axonemal microtubules or the membrane-associated microtubule structure formed during cytokinesis in very late schizont stages. Further, colocalization between alpha-tubulin and kinesin-5 in schizont-stage parasites is not complete indicating a preferential decoration of certain sections of the microtubule structures (possibly the microtubule ends), which could only be resolved by super-resolution microscopy. Using a live cell dye, such as SPY555-tubulin, which directly binds to microtubules will provide a uniform labelling of any microtubule species and hopefully prove useful to the field in the future. Lastly, we present time-lapse microscopy analysis of blood stage cells, contrary to single time point images of live cells, providing a quantified chronology of microtubule reorganization at single cell level (with time stamps). Therefore, we feel that our claim, although it should be relativized, is formally speaking accurate.

      It is also important that authors give valid discussion about previous studies on hemispindle, microtubule dynamics with respect to schizogony (PMID: 18693242; PMID: 11606229; PMID: 33154955) rather than giving the impression that they have given this concept first time on hemispindle dynamics and centrin location during schizogony.

      We agree that those studies should be discussed in more detail. We are grateful to the reviewer for pointing out the Fowler et al. 2001 (PMID: 11606229) study. They use an antibody against gamma-tubulin to demonstrate its presence at the apical pole of subpellicular microtubules (f-MAST) in the merozoite and cytokinetic stages (line 102). However, we were unable to reveal a specific gamma-tubulin staining using the antibody used by them in the preceding schizont stage. After trying many different commercial gamma-tubulin antibodies and attempting to generate our own we now finally observe a gamma tubulin localization at the poles of intranuclear spindles in schizont stage, although the only successful antibody still displays some background staining, possibly including cross-reactivity with alpha or beta-tubulin (Fig. S4, line 237).

      The highly insightful study by Mahajan et al. 2008 (PMID: 18693242) indeed suggests that centrin localizes away from the DNA and demonstrate the distinct localization from tubulin. They, however, likely due to the resolution limit of their microscopy techniques, speculate that the centrin signal is embedded in the membrane, while we could show by super-resolution and nuclear pore staining that centrin is distinct from the membrane (now Fig. 2A; line 257). The work done by Zeeshan et al. 2020 (PMID: 33154955) nicely shows dynamics of kinesin-5 in nuclear division. In schizont stages Kinesin-5 signal elongates and splits alongside the mitotic spindle with which it overlaps for the most part. Colocalization with centrin is less strong although the authors note some overlap. Our data suggest that centrin and tubulin are clearly distinct. In male gametes the authors show nicely time-resolved data of kinesin spreading along the elongating spindle, although hemispindles are not observed at this stage. We introduce and discuss these findings (lines 123, 432).

      The concept of bipartite centrosome is already been discussed in Toxoplasma and the claim by authors in Plasmodium presented here is not substantiated experimentally. They showed that centrin is part of outer region while they do not show with any marker for the inner region. It will be very helpful if the authors use gamma tubulin or MORN1 to show the location with respect to centrin and microtubule. In the absence of this localisation the claims are preliminary and speculative. If the centrosomal protein complex is not involved in microtubule nucleation, then how the nucleation is happening. What are the molecules present in this amorphous matrix? It will be great to check the location of gamma-tubulin or some inner centrosome molecules described in Toxoplasma that is deemed to be MTOC.

      We share the opinion that our Plasmodium data should be compared to Toxoplasma, while still being assessed independently. Despite Toxoplasma belonging to the apicomplexan the conclusion that their centrosomes should be organized in a similar fashion is by no means self-evident considering for example their significant evolutionary distance. Actually, several noteworthy morphological differences have already been well documented. i) Toxoplasma MTOC does contain centrioles in the outer core which is coherent with the centrin and gamma-tubulin localization in this region. ii) Toxoplasma MTOC contains an additional nuclear membrane protrusion enclosing the inner core. iii) mitotic microtubules in Toxoplasma are thought to penetrate the nuclear membrane to connect to centromeres. iv) the inner and the outer core are both extranuclear and therefore not to be equated with the intranuclear compartments. We now expand a bit on the discussion of the aforementioned differences (line 382). Nevertheless, we thank the reviewer for making us realize that the term “bipartite” is a poor choice to describe the centriolar plaque organization in this context. Therefore, we replaced it in the abstract (line 29) and the main text (line 375).

      We acknowledge the fact that it would be desirable to show a marker localizing to the intranuclear compartment, and not only through visualizing the microtubule nucleation complex (Fig. 4A-B) and the positioning of the microtubule ends in this region (Fig. 3A). Concerning MORN1 we found no indication in the published localization data that it is, like in Toxoplasma, associated with the nucleus in Plasmodium species, where it is only found associated with the budding complex (and we are currently unable to procure an antibody) (line 422). We have attempted gamma-tubulin visualization on many occasions throughout the project (transgenic parasite lines, commercial antibodies, self-made antibodies) and only recently found an antibody revealing some specific signal. Indeed, we found localization at the poles of the spindles i.e. the intranuclear compartment (line 237). Unfortunately, this “best-possible staining” still showed some unspecific spindle staining likely resulting from cross-reactivity with alpha- or beta-tubulin causing us to put these data into the supplements (Fig. S4).

      We had more luck with attempting a “new” type of staining, recently used in Plasmodium (Bertiaux & Balestra et al. 2021) using a fluorophore-coupled NHS-Ester in expanded samples. This chemical unspecifically stains proteins and revealed that the centrosomal region contains an exceptionally protein dense “hourglass-shaped” structure (Fig. 3F-H). Since the outer part of this structure colocalizes with centrin and the inner part overlaps with microtubules we assume that the centrosomal complex stretches throughout the nucleo-cytoplasmic boundary and fills part of the intranuclear compartment (line 320). Especially the highly protein dense region at the neck of the “hourglass” seems very coherent with the nuclear membrane embedded electron dense region which can be seen in electron microscopy (e.g. Fig. 3E & 4B). We feel that this staining strongly supports the presence of this novel intranuclear compartment.

      The expansion microscopy is very nice and some of it presented in supplementary can be moved to main section.

      Thanks for sharing our enthusiasm about this imaging technique. We have now selected a representative image of a hemispindle and mitotic spindle stage nucleus imaged by U-ExM and added it to the main section (Fig. 2B, line 231).

      The localisation CenH3 is bit puzzling as it has been shown that centromere/ kinetochore cluster and are present during early and mid schizogony. The various foci with respect to nuclei are not what has been seen previously. Please discuss the difference in these two findings.

      The localization pattern can easily be explained by the increased resolution of STED nanoscopy used in this study. Previous studies (e.g. Hoeijmakers et al. 2012 and Zeeshan et al. 2020) used classical confocal microscopy. Under those imaging conditions the individual foci seen here can´t be resolved and would, in accordance with the other studies, appear as one cluster. We slightly modified the text for more clarity (line 247).

      Reviewer #2 (Significance (Required)):

      • Describe the nature and significance of the advance (e.g. conceptual, technical, clinical) for the field.

      * This is more technical advancement on the subject of centrin by using STED, tomography and CLEM.

      • Place the work in the context of the existing literature (provide references, where appropriate).

      * This work has relevance relation to cell division during schizogony in asexual stages in par with Toxoplasma or in Apicomplexa in general

      • State what audience might be interested in and influenced by the reported findings.

      Working with Apicomplexa, Protist, cell division and mitosis.

      • Define your field of expertise with a few keywords to help the authors contextualize your point of view. Indicate if there are any parts of the paper that you do not have sufficient expertise to evaluate.

      Working on Cell division in Plasmodium.

      **Referee Cross-commenting**

      I agree with the reviewers and some of the experiment suggested and the minor details have to be addressed. There are some loose ends and these suggestions will enhance clarity of the data. It is a very nice study and some of the comments suggested by reviewers will improve the manuscript. __

      Reviewer #3 (Evidence, reproducibility and clarity (Required)):

      **Summary:**

      The centrosome is the primary microtubule-organizing center (MTOC) in eukaryotic cells that nucleate spindle microtubules necessary for chromosome segregation. In most eukaryotic cells, the canonical centrosome is composed of centrioles surrounded by an electron-dense proteinaceous matrix named the pericentriolar matrix (PCM) competent for microtubule nucleation mitotic spindle assembly. Following the breakdown of the nuclear envelope breakdowns, the mitotic spindle microtubules gain access to the kinetochores of the condensed mitotic chromosomes. Once the mitotic spindle is fully developed, centrosomes are at opposite poles of the cells, and chromosomes are pulled toward opposite poles. Cell division completes with cytokinesis resulting in the active formation of two nuclei within two daughter cells. Interestingly, during its asexual replication cycle, the malaria parasite Plasmodium falciparum undergoes multiple asynchronous rounds of mitosis with segregation of uncondensed chromosomes followed by nuclear division within an intact nuclear envelope. The multi-nucleated cell is then subjected to a single round of cytokinesis that produces dozen of daughter cells. We know about the Plasmodium centrosome is that it is made of an acentriolar structure embedded in the nuclear envelope and serves as MTOC during cell division. However, the biogenesis and regulation of the Plasmodium centrosome are poorly understood. Given the peculiarity of the cell division in Plasmodium parasites, understanding the molecular mechanisms that drive and regulate MTOC duplication and maturation could unveil novel targets for the treatment of malaria. In this study, Simon et al. successfully applied challenging and cutting-edge microscopy techniques to monitor the dynamic formation of the spindle microtubules and MTOC during Plasmodium intraerythrocytic mitosis. In addition, they remarkably combined stimulated emission depletion (STED) with ultrastructure expansion microscopy to define an uncharacterized intranuclear compartment devoid of chromatin as the nucleation site of nuclear microtubules. And lastly, the authors adapted an in-resin correlative light and electron microscopy (CLEM) approach to define the centriolar plaque position in a novel intranuclear compartment with centrosomal function.

      **Major comments:**

      1. In the methods section, it is stated that across this study, three different anti-tubulin antibodies (alpha-tubulin B-5-1-2, alpha-tubulin TAT1, beta-tubulin KMX1) were used, and two anti-centrin antibodies (TgCentrin1 and PfCentrin3) were used, one of which seems to have been generated in this study (anti-PfCentrin3). It is unclear in the figures or results section when each of these antibodies was used, and the authors should give a rationale for using multiple antibodies in combination.

      To label microtubules we used the mouse anti-alpha-tubulin B-5-1-2 (Sigma, T5168) antibody throughout the study. Except for U-ExM were we added two additional primary antibodies against tubulin. Due to the expansion of the samples the antibody binding epitopes are stretched out in space. This causes a significant reduction of local epitope concentration (expansion factor 4.5 in all directions results in ~ 80-fold increase in the volume), which can reduce the signal intensity. Adding multiple antibodies binding different epitopes of tubulin can compensate for this dilution effect to some degree, as has been shown before by Gao et al. 2018. At the same time the expansion contributes to the accessibility of the usually densely packed tubulin epitopes within the microtubule polymer, which certainly adds to the success of U-ExM. What the respective contributions of those effects are is not clear, but we found superior signal-to-noise ratios when combining three tubulin antibodies instead of using one. The TgCentrin1 antibody was only used in Fig. 2C (now Fig. 3B) and validated the localization pattern of our new PfCentrin3 antibody we used in the other pictures. We now provide clearer description of antibody usage in the methods section and a new supplemental table.

      The anti-PfCentrin3 antibody seems to have been generated for this study. If this is the case, the authors should provide evidence that this antibody binds to the recombinant PfCentrin3 it was raised against and binds PfCentrin3 in parasite lysates.

      The anti-PfCentrin3 antibody was, indeed, produced for this study and we should have provided our western blot data right away. We now show the requested blot, which shows bands at the appropriate size in parasite lysate as well as for the recombinant protein, in the supplements (Fig. S2, line 178).

      In the first paragraph of the Results section, the authors' remark of centrin foci that they are "...only detectable later (Mov. S2) or sometimes not at all." In Figure 1 A-C, it is implied that the first observed division is the first nuclear division of that parasite. Given that some nuclei do not have a visible centrin focus, it cannot be concluded with certainty that these parasites only contain a single nucleus and that this is their first division. The authors would need to include a quantifiable DNA stain to show this unequivocally to show a single nucleus. It has undergone DNA replication, similar to Klaus et al., 2021 BioRxiv paper. In the absence of a DNA stain, the authors should reword to clarify that this is the first observed division and speculate that it is the first division of that nucleus, but the authors should draw no firm conclusions about the first division.

      Indeed the variability in protein levels that can result from exogenous expression can lead to some cells not showing clear Centrin1-GFP foci. Although this is a rare event we wanted to acknowledge this observation. The live cell microtubule staining using Spy555-Tubulin we use is, however, highly specific and sensitive and would stain any nucleus undergoing division including the first one. If there would be more than one nucleus in the observed cell it would unequivocally show two clearly separated tubulin signals (hemispindle or mitotic spindle). To illustrate this we added Fig. 1B (line 148) showing two live parasites stained with SPY555-Tubulin plus a Hoechst-based dye showing one or two nuclei alongside the corresponding tubulin signal. We modified the text to clarify how we stage the parasite for time-lapse acquisition (line 154). We already extensively experimented with state of the art fluorogenic live cell DNA dyes (e.g. from Spirochrome and the Johnsson group) to visualize the nuclei directly in time lapse microscopy, but even at minimal concentrations they all significantly inhibit mitotic progression. We also add this information in the main text (line 150).

      In the first paragraph of the Results section, the authors write: " We quantified the duration of hemispindle, accumulation and anaphase stages ...." Anaphase spindle fibers means that the sister chromatids are separated. In the absence of a centromeric marker like NDC80, it doesn't seem easy to claim the anaphase stage. The authors should write " extended spindle." The authors might also consider using the term collapsed spindle instead of accumulation to reflect the dynamic of the intranuclear microtubules during the blood-stage replication. The same modification should be made for Figure 1B, so we read " hemispindle, collapsed spindle and extended spindle."

      We thank the reviewer for this suggestion, which is very much in line with a comment by Reviewer 1 on the definition of anaphase. We acknowledge that the term is ill-defined here. Further, it suggest a mitotic morphology analogous to the one observed in “classical” models (prophase, metaphase, anaphase,…), which is not fully appropriate. Consequently, we decided to adapt the suggested terminology in Fig. 1 (and also new Fig. 2) and in the text (line 160).

      Based on the evidence in this study, it cannot be stated unequivocally that the centrosome is entirely extranuclear, at least not as it is implied in Figure 3C. In Supplementary Figure 4, the microtubules appear to be extruding from a circular structure that may either be intranuclear or span the nuclear envelope. In Supplementary Figure 6, the structure pointed to as the centrosome appears to be embedded within the nuclear membrane with a top structure on the cytosolic side of the nuclear envelope. Thus, the best support for an extranuclear centrosome comes from the CLEM images. Still, it is noteworthy that the double membrane of the nuclear envelope is not visible on this slice in the region where the centrin fluorescence is found. Considering some of the fluorescence pixels for centrin are outside the parasite plasma membrane, and some of the Hoechst pixels are outside the nuclear envelope, this data does not show unequivocally that centrosomes are entirely extranuclear. However, this argument would be strengthened if the authors performed a proteinase K protection assay (or something similar) to determine if Centrin1 and Centrin3 are exposed to the cytosol. However, in the absence of that or further evidence, the authors should dampen their claims about the centrosome being exclusively extranuclear, as represented in the schematic in figure 3C.

      We thank the reviewer for this comment, which highlights an issue in our communication of our working model of the centriolar plaque. At no point we intended to claim that the centrosome is exclusively extranuclear. Rather, centrins, which are currently the only reliable marker proteins, localize to a subcompartment of the extranuclear region of the centriolar plaque. Additionally, the centrosome clearly contains an intranuclear region. The composition of this intranuclear compartment is elusive, except that it harbors microtubule nucleation sites. Indeed, our model in Fig. 3C (now Fig. 4C) is misleading and not well annotated. The newly added NHS-Ester staining fortifies this claim (Fig. 3F-H. Consequently, we corrected our working model by adding an explicit figure labelling (now Fig. 4C).

      We apologize for the misleading labelling in Fig. S6 (now Fig. S7). The green arrow was intended to point out the electron dense region associated with the nuclear membrane, which has been seen in previous studies, and was not intended to represent the entire extended centriolar plaque. If anything, this smaller region might provide the link between the intra and extranuclear compartments that the reviewer also identified in Suppl. Fig. 4 (now Fig. 2D). We modified the annotation of the Fig. S7 and Fig. 4A-B accordingly, labelling it the “electron dense region”. More importantly, we hope that our newly added data using NHS-Ester staining of protein dense regions (Fig. 3F-H) highlights the spread of the centrosome across the nucleo-/cytoplasmic boundary more clearly.

      Considering whether centrin is actually extranuclear, we feel that the data shown in Fig. 2A (now 3A) is convincing. We have, however, added two panels of the relevant regions showing centrin localization respective to the nuclear pore and adjusted the contrast as we acknowledge the limited “visibility” within the unadjusted panels. The fact, that the centrin signal slightly overlaps with the nuclear envelope in CLEM images can be explained by the relatively poor resolution of the widefield microscope we had to use to image the sections. From the other super-resolution images in the manuscript, we know that the perimeter of the better resolved centrin signal is significantly smaller. Otherwise one had to assume from the CLEM data that centrin is also in the cytosol of the red blood cell and that DNA is localized outside the nucleus. On a similar note the fluorescence image is, contrary to the tomography image, a single slice since the thickness of the sample section (about 200nm) is significantly below the z-resolution (about 500nm) of a fluorescence microscope.

      Throughout the study, the level of biological replication is unclear. The authors rigorously include all the data points for each of their graphs and the total number of images/videos quantified. And what needs to be added, in either the figure legends or a methods section, is the number of biological replicates for each of these measures came from.

      We have added the number of replicas in the figure legends.

      **Minor comments:**

      STED is present as an acronym in the abstract and should be spelled out in full and clarified that it is a super-resolution microscopy technique.

      We opted to remove STED from the abstract (leaving it at super-resolution, which includes expansion microscopy) to avoid disrupting the “flow” of the abstract and now spell out the acronym at the first mention in the introduction (line 127).

      The second paragraph of the Results section states that ring and early trophozoite stage parasites do not express tubulin or centrin. Still, only an early trophozoite is shown in Supplementary Figure 2. Therefore, the authors should either include a similar image of a ring-stage parasite or remove ring-stage parasites from that statement.

      We have removed the ring stages from the statement.

      The second paragraph of the Results section contains the sentence, "At which point tubulin is reorganized into the bipolar microtubule array, which then forms the mitotic spindle cannot be resolved here." The authors are implying that the point at which tubulin is reorganized into the microtubule array, which goes on to form the mitotic spindle, cannot be resolved here. This is not particularly clear, though, and this sentence could be reworded for clarity.

      We reformulated the sentence to clarify the point we failed to make with the previous wording (line 188).

      The second paragraph of the Results section contains some statements about the results without referencing the figures that these statements come from. The authors should clarify this to make clear which figures each statement refers to.

      We added more references to the appropriate figure throughout the paragraph (lines 188, 219, 223).

      In the third paragraph of the introduction section, the authors write, " Centriolar plaques seem partially embedded in the nuclear membrane, but their positioning relative to the nuclear pore-like "fenestra" remains unclear." Unfortunately, the lack of reference did not allow me to understand if the authors state literature or comment on past published results.

      We added the reference which was incorrectly positioned before the sentence instead of at the end (line 82).

      the authors could add some references:

      • Second section of the introduction: " the 8-28 nuclei are packaged into individual daughter cells, called merozoites ( Rudlaff et al. 2019 PMID: 31097714)

      • Third section of the introduction: " The centrosome of P.falciparum is called centriolar plaque" ( Arnot et al. 2011, Sinden 1991a); " the nuclear pore-like "fenestra" remains unclear (Wall et al. 2018; Zeeshan et al. 2020).

      • Fourth section of the introduction: " tubulin antibody staining are extensive structures measuring around 2-4um ( Ref?)

      • When the authors introduce subpellicular microtubules of segmented schizonts, a reference to a study that shows these structures should be included.

      • A previous study that shows the distinct structure of microtubule minus ends should be cited when this structure is described.

      • Third section of the results, the authors should cite Bertiaux et al. 2021 with the Gambarotto et al. 2019 paper regarding U-ExM.

      We apologize for missing some important references or putting them in the wrong position. We now added all the references or cite them again at the appropriate locations throughout the text.

      Figure 1E shows hemispindle and mitotic spindle lengths of U-ExM expanded parasites, but the position within the figure and figure legend implies that these lengths were determined unexpanded parasites. Therefore, it should be stated in the figure legend that these measurements come from U-ExM expanded parasites. Moreover, I encourage the authors to include U-ExM images in the main figures. The images are beautiful, represent a significant technical achievement, and directly relate to Figure 1E. To the best of my knowledge, this is only the second study to perform expansion microscopy on Plasmodium and the first to use PFA-fixed parasites and a nuclear stain. It would be valuable for the Plasmodium and ExM communities to see this technical advancement represented in the main text.

      We thank the reviewer for the appreciation of our ExM data and added it to Fig. 2B before the quantification of the microtubule length and number and added the information to the legend.

      In the second paragraph of the Results section, the authors write, " but clearly display the microtubule cytoskeleton associated with the inner membrane complex." It would bring clarity to define in few words what the IMC is.

      We included a short definition of the IMC (line 223).

      The methods section details that the length of microtubules was determined by dividing the observed values by an expansion factor of 4.5. If the authors recorded the expansion factors of their gels, this data should be included, and how it was recorded should be stated in the methods. If not, the authors should include the rationale of using an expansion factor of 4.5 as this is slightly different from the previously published expansion factor of P. falciparum of 4.3.

      We recorded the expansion factor by measuring the gel size pre and post expansion with a ruler and found a factor of 4.5 on average. We added this information in the methods (line 688).

      There are several parasite lines used in this study, and some figures are not clear what parasite line was used. Could the authors please include the parasite lines in the figure legends of Figure 1 D-F, Figure 3, Supplementary Figures 1-2, and Supplementary Figures 4-7?

      We added the parasite line information in the legends as requested.

      Nuclear pore complexes, of which Nup313 is a component, can have cytoplasmic, integral, and nuclear-facing components. If it has been shown previously that PfNup313 is the homolog of Nup214 in vertebrates present on the cytosolic side of NPC, this should be stated. If not, then it should be clarified that it is unknown whether Nup313 faces the cytoplasm, nucleus, or is embedded in the NE, as this has implications for the colocalization of Nup313 and Centrin.

      Nuclear pore proteins are very poorly conserved in P. falciparum and Nup313 has only been recently identified as such (Kehrer et al. 2018) mainly by the presence of FG-repeats (as for all the other newly defined proteins). The only related ortholog that can be found through BLAST search against humans, yeasts, and Arabidopsis is Nup100 from S. cerevisiae. ScNup100 is a central pore localizing protein but the sequence similarity to Nup313 is low. We are not aware of any findings showing relatedness to vertebrate Nup214, while sequence analysis rather indicates the absence of orthology. To clearly demonstrate the individual positioning of the few known Nups within the parasite´s nuclear pore complex would require a dedicated long-term project. However, due to the presence of FG-repeats one can assume that it is part of the central FG-Nups layer rather than of the intranuclear basket or the cytoplasmic filaments (line 255). Therefore it would localize more closely to the nuclear envelope than the latter. Either way, a clear gap between centrin and Nup313 signal can be identified and colocalization has not been observed. These data indicate that the exact position of Nup313 on the cytoplasmic, integral or nuclear-facing site is not decisive for the conclusions made in this study and our observations preclude scenarios where centrin is not extranuclear.

      It seems from the image in Figure 2C that DRAQ5 and Hoechst have at least visually indistinguishable localizations. Have the authors taken any STED deconvolved images of nuclei stained with both Hoechst and DRAQ5? Considering the striking increase in detail of the Hoechst signal in STED deconvolved images, it may be informative both to this study and to people who work on chromatin organization what the chromatin staining looks like in the absence of bias towards chromatin state.

      It would, indeed, be interesting to analyse chromatin organization by those means, but DRAQ5 is not a STED compatible dye, highly prone to bleaching, and therefore not suitable for such analysis. Being an infrared dye DRAQ5 is compared to the UV excited Hoechst also yielding a reduced spatial resolution, which is limited by the emitted wave length.

      For the tomography and TEM images, the centrosome is indicated with an arrow, but it isn't entirely clear what that arrow is pointing to for some images. It would be clearer if the centrosome were outlined in green, like the NE, rather than just an arrow. This is particularly important for Supplementary Figure 4, where to my eye, it appears that the microtubules inside the chromatin-free region are coming directly out of a circular structure, which could be interpreted as the centriolar plaque.

      The reviewer is right to point out the use of arrows for centrosome annotation. It was intended for orientation of readers to indicate the “likely position of the centriolar plaque” since a clear boundary around the centrosome can´t be defined. It would have been more precise to indicate that the arrow is pointing at the electron dense region associated with the nuclear membrane, which is of course only one of the sub-regions of the centrosome. This is particularly important since we want to emphasize the extended dimensions of the centrosome. Consequently, we modified the annotation to “electron dense region” in all concerned figures and corresponding legends.

      The ordering of Figure 2A-C seems to imply that the DNA-free region was measured in the STED deconvolved images, but the methods imply that it was in the confocal images. The authors should clarify this in the figure legend or by rearranging B and C's order.

      Hoechst signal was indeed acquired and measured in confocal mode and to avoid confusion we have changed the order of the figures (now Fig. 3B-C) as suggested.

      The authors should provide some more detail on how the DNA-free zone was measured. For example, was it measured on single slices or maximum intensity projections? Was it measured from the middle, far, or near side of the centrin focus? Etc.

      The measurement was carried out in the slice where the DNA-free zone was in focus. Depth was measured from below the centrin signal until the “bottom” of the DNA-free zone. We hoped that the little schematic above the figure would clarify this question, but acknowledge the need to more clearly explain the measurement method, which we now do in the corresponding figure legend (Fig. 3C).

      The methods state that the mCherry signal in figure 2C was detected using a mCherry nanobody. This should be clarified in the figure legends as it currently seems as if we see endogenous mCherry fluorescence.

      The visible signal is certainly a combination of the mCherry plus the “boosting” effect from the Atto594-coupled nanobody that we added. Clearly, this should be mentioned in the figure legend, which we now do.

      The data in Supplementary Figure 4 seems vital to the interpretation of the study. Therefore, for clarity, I encourage the authors to include Supplementary Figure 4 in Figure 2.

      We share the reviewers view on these data and moved them to the main figures (now Fig. 3D).

      In the last sentence of the discussion, it is unclear what the authors mean by how the nuclear compartment "splits," could they please clarify?

      We were referring to the event of centrosome duplication, which has to occur during nuclear division. In a structure without centrioles or a spindle pole body structure forming a half bridge we therefore need a new model to explain how the two poles of the spindle are formed. Potential modes are splitting or de novo assembly. This aspect, as also pointed out by other reviewer, warrants a bit more explanation, which can now be found in the discussion (line 468).

      If the pArl-PfCentrin3-GFP plasmid or pDC2-cam-coCas9-U6.2-hDHFR have been published previously, the respective studies should be cited. If not, the study where the vector backbones were first established should be cited.

      We have now cited the original studies publishing the vector backbones for the first time in the methods (lines 490, 501).

      From the current text, it is not clear that the Nup313 tagged parasites also had a GlmS ribozyme. It is shown in Supplementary Figure 3, but the authors should clarify either in the text of the results, or figure legends, that this parasite line was Nup313_3xHA_GlmS

      The Nup313-tagged line indeed has a glms ribozyme after the HA-tag, which we now mention in the figure legends.

      In the plasmid constructs section of the methods, the authors list several primers by number but not by sequence. Instead, the authors should include the sequence and orientation of each of the primers mentioned in a table as supplementary data.

      This is a good suggestion. We have generated a table at the end of the supplementary data file and on this occasion we also added tables of all the antibodies and dyes used in this study.

      The authors should cite the study where the TgCentrin1 antibody was generated and provide the Rat anti-HA 3F10 antibody catalog number, as catalog numbers are provided for other commercial primary antibodies.

      We now provide the missing catalog numbers in the supplemental data table.

      There is an issue with the formatting of the journal-title in the Kukulski et al. reference.

      Thank you for noticing this error, which we now corrected.

      Reviewer #3 (Significance (Required)):

      The genome of P. falciparum is fully sequenced; however, over 50% of encoded proteins are of unknown function, with many of these proteins unique to Plasmodium parasites. By identifying and characterizing essential biological processes, especially those divergent from human host cell processes, we will formulate ways to interfere with them by developing novel antimalarial drugs. The process of Plasmodium cell division differs from the classical cell cycle of its human host. In the study led by Caroline Simon, authors successfully utilized recent developments of super-resolution microscopies on expanded parasites to identify novel features of cell division machinery of the malaria blood-stage parasite.

      Simon et al.'s work highlight the growing interest in the diversity of cell division mode of Apicomplexan parasites, which will likely contribute to a deeper understanding of the origin and functional role of the centrosome in eukaryotic life. In 2020, the Open Biology journal published a unique article collection named Focus on Centrosome Biology showcasing research that advanced our knowledge on centrosome function, evolution and abnormalities. In addition, the reported findings will interest research groups studying cell cycle regulation and evolution beyond the field of parasitology.

      Our lab studies the peculiar cell cycle of Plasmodium falciparum to gain a functional understanding of mechanistic principles of nuclear envelope assembly and integrity during the cell division of the human malaria parasite.

      **Referee Cross-commenting**

      It is a wonderful study, and once all reviewer's comments are addressed, the manuscript should be in excellent shape for publication.

  10. Jan 2021
  11. Dec 2020
  12. Oct 2020
  13. Jul 2020
    1. Note: This rebuttal was posted by the corresponding author to Review Commons. Content has not been altered except for formatting.

      Learn more at Review Commons


      Reply to the reviewers

      We thank the reviewers for their comments and outline below how we plan to address them.


      Reviewer #1 (Evidence, reproducibility and clarity (Required)): **Summary:** Provide a short summary of the findings and key conclusions (including methodology and model system(s) where appropriate). The authors here describe a method to modify bacterial artificial chromosomes (BAC) harbouring gene loci from eukaryotes. When wanting to modify a BAC an antibiotic selection cassette is often included alongside the desired mutation/modification to increase the number of successful recombinants in E.coli. Traditionally, this is removed in a second recombination process to leave only the desired modification. The novelty in the procedure described herein is to add a synthetic intron consensus sequence around the selection cassette, which eliminates the need for the subsequent removal of the antibiotic cassette from the BAC before transfection into mammalian cells, saving time and resources. The technique is clever in its simplicity and appears to function for a number of gene loci. The authors validated the correct functioning of the modified BACs for a number of genes using three main assays - transcript level, protein level and localisation. **Major comments:** *Are the key conclusions convincing?* The conclusion that the method described generates functional modified BACs is valid. *Should the authors qualify some of their claims as preliminary or speculative, or remove them altogether?* While the method is successfully employed in this study, its efficiency is not quantified in relation to the state-of-the-art as described in the introduction. One assumes it would be more efficient, but this has not been tested empirically in the paper. Does the inclusion of the synthetic intron sequence have an effect on the efficiency of modifying BACs compared to a more typical two-step positive/negative antibiotic selection cassette? *

      • *

      This is a good point that we did not directly address. In general, the efficiency is similar to that of integrating any cassette with selectable marker, as has been published (Poser et al 2008), and therefore also higher than the two-step counterselection method, which requires such a cassette integration in the first step alone. We will include new data specifically addressing the efficiency of our new method (see specifics below)

      The functionality of this approach rests entirely on the ability of the target cell to correctly splice out the synthetic intron. The authors are aware of this potential problem as highlighted in the lines below, but do not make efforts to explicitly test splicing. On lines 224-225, the authors state "We cannot exclude that a small portion of synthetic introns within individual cells are misspliced". On lines 230-231 it is stated that "mis-spliced mRNAs are probably minimal and degraded by nonsense-mediated decay". On lines 215-217, the authors describe an "investigation of transgenic lines at the single-cell level" that suggests "the synthetic intron is correctly spliced out in all the cells of the population". How do the authors reach this conclusion? U2OS and HeLa cells are considered very "robust" and may not show detectable consequences when stressed with an increased level of nonsense-mediated decay. Further, many genes maintain a high level of expression that buffers them against small changes in transcription/splicing. The synthetic intron might have a bigger impact on more tightly regulated genes, so assessing the splicing rate would be essential if the authors wish to advocate their technique as generally applicable.

      • *

      We will assay for splicing efficiency as outlined below.

      The ability of the synthetic intron to be removed from final transcripts depends on functioning splicing machinery. The authors might emphasise this issue, as spliceosome mutations are important fields of study and might not be compatible with this method.

      • *

      We can add this in the text

      The authors used un-directed integration of each BAC under study. Therefore, it is hard to assess what effect the synthetic intron has, as the authors only ever assess the downstream levels of the correctly spliced, translated and localised protein. The authors themselves state that this can lead to clonal variations in expression of up to 2-fold and on line 250 that this variation "could compensate for synthetic intron effects", but make no effort to test this. Again, lines 267-268 highlight the potential dangers of potential effects of the synthetic introns, but do not test these. \Would additional experiments be essential to support the claims of the paper? Request additional experiments only where necessary for the paper as it is, and do not ask authors to open new lines of experimentation.* If not already performed, a large number of bacterial colonies should be screened for the correct modification and frequency of correct ones reported. This frequency - reported for at least three different modifications - would estimate what sort of efficiency this method provides. The modified region of each BAC should be sequenced and the results reported. The rate of exactly modified clones is important, in case of spontaneous or low fidelity integration of the antibiotic cassette. The percentage of transcripts that have the synthetic intron correctly spliced out should be measured for some of the BAC constructs used in the study. A direct head-to-head comparison of this newer method compared to other techniques, or even the authors' own previous two-step approach is necessary to assess the benefits of this method. Preferably, the experiment would be run in parallel with and without antibiotic selection applied, to show that it drastically improves chances of finding a correct clone. *

      We will generate 3 new mutations in BACs and analyze both the efficiency of integration by PCR and accuracy via sequencing. In practice, we have observed that the efficiency is similar to any other cassette integration, such as a GFP tag (Poser et al Nature Methods 2008) or a counterselection cassette (Bird et al Nature Methods 2012) (80-90%). Integrating a mutation via the second step of the counterselection method introduces a further 20% decrease in efficiencies on average.

      \Are the suggested experiments realistic in terms of time and resources? It would help if you could add an estimated cost and time investment for substantial experiments.* Repeating the transformation of the BAC and targeting cassette and assessing the recombination efficiency and sequencing should only require existing reagents and take less than a week or two to complete. Quantitative RT-PCR to assess the percentage of transcripts that have the synthetic intron spliced out would take a little more work. However, this should not be a considerable investment in time or resources for a standard microbiology laboratory and could be completed within a few weeks using modern techniques, such as that described in Londoño et al. 2016. Repeating all the experiments in parallel would be considerable work and would only be strictly necessary if the authors wish to emphasise the benefits of their method over the many others already in wide use. *

      • *

      We will use quantitative PCR to estimate the fraction of transcripts that correctly splice out the artificial intron for two clonal cell lines characterized in the study: RNAi-resistant AurA-GFP (Fig 4), and GTSE1-14A (newly introduced; see below). While the exact method described in Londoño et al 2016 will not be applicable due to the larger size of the artificial intron, we believe we can adapt it to detect different splicing events.

      \Are the data and the methods presented in such a way that they can be reproduced?* Barring the omission of Table S1, which presumably includes exact information on the BACs modified and sequences used etc., there is sufficient other data and methods to allow the experiments to be repeated. Targeting the ESI procedure to the middle of exons is likely to have a bigger impact for smaller exons as the authors mention on lines 99-100. Making it clear which exon sizes for each gene were successfully targeted in this study would help give some idea of how significant a problem this might be. Perhaps Table S1 contains this information, but it was not provided. It would also help reviewers check the design strategies. *

      We apologize for inadvertently failing to upload Table S1 on bioRxiv. It has been uploaded now as part of this submission process. This table indeed contains BAC and target sequence information, including the size of the targeted exon (and the 2 “new” resulting exons). Targeted exons range in size from 138bp to 1537bp, and “new” exons are as small as 48bp.

      \Are the experiments adequately replicated and statistical analysis adequate?* The replication and statistically analysis of the data as presented appear adequate. Figure Legends should state the statistic used to generate error bars. *

      This will be updated

      \*Minor comments:** Specific experimental issues that are easily addressable. Are the promoters used in the vectors described universally functional? For example, is the PGK promoter functional in yeast? *

      • *

      The PGK promoter contained in the cassettes is a mammalian promoter, which has also been reported to work in flies.

      \Are prior studies referenced appropriately?* The manuscript may benefit from the referencing of BAC modification techniques from a wider variety of groups, such as those using CRISPR-guided recombineering (Pyne et al. 2015). *

      We will add citations of more techniques

      \Are the text and figures clear and accurate?* The body text is very clear save minor typographical or grammatical errors. Regarding figures, some of the coloured text in Figure 1 is somewhat illegible when printed in grayscale. Line 278 - The acronyms LAP and NLAP are not defined/explained. Antibody section starting Line 282 may fit better next to Western Blot section. Figure 2C - The blot images would benefit from arrows to indicate expected sizes of proteins. Figure 3A - the graph may benefit from a dashed line at 100% to highlight that values are normalised to controls. Figure 4 - The differences between panels B & C are unclear. Figure 4E - The legend could provide a little more detail on cell cycle stage/status of the captured cells. *

      All of the above will be addressed accordingly

      \Do you have suggestions that would help the authors improve the presentation of their data and conclusions?* Lines 23-27 are somewhat unclear and feel out of context. Perhaps the authors could clarify this as a further advantage of using BACs instead of endogenous gene modifications. *

      Thanks for the input, we will clarify this.

      While not affecting the factual content of the paper, I would advocate that the authors format the method described in Figure S3 into a more detailed text based layout similar to that seen in a typical Nature Methods article. However, this may depend on the format required by any eventual publishing journal.

      • *

      We prefer the graphical protocol, but will discuss whether to add a text protocol with the journal editor.

      That all of the work the paper was carried out in human cell lines and using human genes is a further caveat, but the authors admit this in the discussion and one would assume that most mammalian cells would respond similarly in their ability to splice out the synthetic intron. Reviewer #1 (Significance (Required)): \Describe the nature and significance of the advance (e.g. conceptual, technical, clinical) for the field.* This work is a formal description of a newer method that could be useful for many of those employing bacterial artificial chromosomes in numerous studies, such as gene regulation. *Place the work in the context of the existing literature (provide references, where appropriate).* This work builds on methodology previously published by the authors - a counter-selection two-step procedure (Bird et al. 2011). It sets out to formally describe a method merely mentioned as "BAC intronization" in a later paper by some of the authors (Zheng et al. 2014). Other alternative one-step procedures are also available, but present a different set of challenges (Lyozin et al. 2014). Some newer approaches, such as those using CRISPR-guided recombineering (Pyne et al. 2015) or systems that combine CRISPR and positive/negative selection cassettes (Wang et al. 2016) may be slightly more efficient, but are also more complex in their design. Bird et al. 2011 DOI: 10/dv776q Pyne et al. 2015 DOI: 10/f7jx92 Wang et al. 2016 DOI: 10/f89db5 Zheng et al. 2014 DOI: 10/f5pkr6 *State what audience might be interested in and influenced by the reported findings.* As a technology paper this work should have interest from a broad field of research. While the use of BACs could sometimes be considered more traditional in light of the explosion in CRISPR-based genome editing capabilities, it is definitely seeing a resurgence as the limitations of CRISPR in modifying large regions of genome become more apparent. Therefore, technologies that accelerate the modification of BACs could prove increasingly useful. As category of audience, all those involved in significant recombineering or gene/genome engineering would potentially benefit. *Define your field of expertise with a few keywords to help the authors contextualize your point of view. Indicate if there are any parts of the paper that you do not have sufficient expertise to evaluate.* Synthetic genomics, synthetic biology, cancer cell biology, gene and genome engineering REFEREES CROSS COMMENTING I would agree with reviewer two's assessment that we both view the paper in a similar light. Reviewer #2 (Evidence, reproducibility and clarity (Required)): This is a methods-focused paper that presents a strategy to efficiently introduce mutations into a bacterial artificial transgene using synthetic introns. BAC-based methods have been an effective strategy for introducing trans genes into human cells to achieve near-endogenous expression, including extensive work from these authors. However, generating mutations and changes within the internal coding sequence presents some challenges for how to target these mutations and select for the mutated form. Here, the authors describe a way to overcome this by introducing synthetic introns into an adjacent sequence. This allows them to introduce a selectable marker and conduct the molecular biology without creating complications downstream for the functionality of the protein. This method is carefully described and presented. The authors also provide clear validation by using this to create RNAi-resistant versions of multiple different mitotic factors as well as creating targeted mutants that alter the functional properties of a protein. This work clearly takes advantage of other ongoing studies from these labs (including mutants and cell lines that appear to also have been described elsewhere), but the ability to combine these in a single paper and clearly describe the method provides a helpful advance and validation. Based on the description and data presented, I think that things are clear and carefully validated. As such, I do not have technical comments or concerns and I would be comfortable with this paper appearing in an appropriate journal in its present form. Reviewer #2 (Significance (Required)): This is a solid methods paper, but for considering the nature of the impact and significance of this paper, there are several things to note: 1.The BAC-based method does appear to be a powerful and effective strategy. However, beyond the work of Mitocheck and the authors that are part of this paper, this has not seen widespread adoption. It is possible that this current method may increase its usage due to the value of the targeted mutations within the coding sequence, but at present it is not a broadly used strategy. *

      We agree that using BACs as transgenes has not seen widespread adoption as a tool on the broader cell biology community (although certainly beyond members of the Mitocheck consortium). This is likely because many erroneously think that it is a technique for specialist laboratories. We are trying to change this! For reasons outlined below, there is still an increasing desire for conditional analysis of mutated genes under physiological expression/regulation frequently not attainable via directed Cas9-based mutation. A major aim of this paper is thus to further simplify the methods for generating modified BAC transgenes.

      2.This BAC-based approach (and also RNAi) are becoming increasingly replaced by the use of CRISPR/Cas9 genome editing. The absence of Cas9-based strategies in this paper limits the potential impact and reach of this paper. The authors do mention the possibility of using a similar synthetic intron strategy for use with Cas9 in the Discussion, and appear to have conducted some experiments. If possible, it would substantially increase the value of this paper if this data and strategy were also included in the Results section (acknowledging that this may still be a work in progress).

      While some uses of BAC transgenes are in some cases better replaced by CRISPR/Cas9 techniques (i.e. GFP tagging), there are several occasions where using BACs are preferable: As stated in the text, RNAi-resistant BACs allow for conditional analysis of recessive mutations. Mutations in essential genes that are lethal will prevent growth and recovery of viable cells if integrated into the genome via Cas9. Additionally, deleterious mutations are prone to accumulate suppressive changes in chromosome integrity or gene expression during the procedure of selecting and expanding Cas9-modified cells for analysis, particularly in the genomically instable cancer cell lines frequently employed.

      We use both BACs and CRISPR/Cas9 in our lab according to our needs.

      We do have an ongoing project to apply this intronization technique to enable more efficient selection of CRISPR/Cas9 integrations. Preliminary results suggest that it works to allow selection of point mutations, but it is still being optimized, including a redesign of the cassette, and is not ready for publication.

      3.The method is solid and well-validated, but there are no new results or insights presented in this paper from the work that is described (this is fine, just commenting for considering the right journal fit).

      As “biological insights” gained as a result of this technique we had cited a couple studies that made use of the technique already (to functionally analyze a microcephaly-associated mutation in the centriolar protein CPAP at the single cell level in HeLa cells and neural progenitor cells (Zheng et al 2014, Gabirel et al 2016)). As a response to this critique to include “new biology” in this paper, we will add new unpublished data investigating a specific question: Is the cell-cycle-regulated disruption of the EB1-GTSE1 (microtubule plus-end tracking proteins) interaction in mitosis required for chromosome segregation fidelity? We have generated a GTSE1 mutant with 14 phosphosites mutated to alanine using this technique. We will present the effect on chromosome segregation.

      REFEREES CROSS COMMENTING It appears that both reviewers are largely on the same page regarding this paper.

  14. Jan 2020
  15. Aug 2018
    1. such as DOIs, which might be assigned by, for example, “crossref” or “figshare”

      I have to say publicly that this sentence makes absolutely no sense as crossref and figshare are not comparable assigning authorities. CrossRef is a registration agency of the International DOI Foundation; FigShare is not. Based upon the example given, the assigning-authority for a DOI would only ever be the set of agencies that assign DOIs. FigShare is not one of those agencies. See it is not on the list: https://www.doi.org/registration_agencies.html

  16. Jan 2016
    1. It is not possible to "capture" your notes and highlights, to organize, compile, arrange, or to print them out. Until there is a seamless way to do this, marginalia will remain sequestered in the margins, and the promise of electronic books will be unrealized"

      Got you there, JD.

    2. One of the great things about the new Web is that you can manipulate text, but the iPad treats you like a child.