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    1. The non-snRNP factors are also necessary for splicing, of which serine/arginine (SR)-rich proteins were considered as markers of splicing speckles (25). We determined whether p.Pro315Leu could affect the pattern of splicing speckles using SC-35, a non-snRNP component, as a marker (25). We performed immunofluorescence and Q-PCR on cells carrying either p.Pro315Leu or WT allele. By confocal microscopy, we found the level of endogenous SC-35 is dramatically increased with a diffused pattern in hPrp4Pro315Leu fibroblasts, whereas in control fibroblasts the SC-35 showed a distinctly speckled pattern (Fig. 4B and C). Consistently, Q-PCR revealed that the expression levels of SRSF1 (encoding SF2/ASF; NM_006924.4), another non-snRNP component and SRSF2 (encoding SC-35; NM_003016.4) were significantly increased in hPrp4Pro315Leu fibroblasts compared with WT fibroblasts (Fig. 4A). Similar changes in the levels and distribution of SC-35 were also observed in ARPE19 and 293T cells transfected with hPrp4Pro315Leu, but not in those transfected with hPrp4WT (Fig. 4D–G), indicating that the p.Pro315Leu variant of PRPF4 affected the splicing machinery.

      ExperimentName: Altered pattern of splicing speckles in patient fibroblasts harboring a heterozygous p.Pro315Leu variant in PRPF4

      PatientCell: CL:0000057 (fibroblast)

      GeneFunction: GO:0000398 (mRNA splicing, via spliceosome)

      GeneAlteration: Cells harbor a heterozygous p.Pro315Leu variant in PRPF4.

      FunctionalEvidence: Patient cells harboring the variant exhibit a much higher level of endogenous marker of splicing speckles (SC-35) with a diffused distribution rather than a pattern of distinct speckles (Figures 4B and 4C). RT-PCR showed increased expression of SRSF1 and SRSF2 as well (Figure 4A). Collectively, the patient cells harboring the variant show molecular evidence of disrupted splicing.

      FAVariants: The model harbors the NM_001244926.2(PRPF4):c.941C>T (p.Pro314Leu) variant in the heterozygous state (ClinVar ID: 143057).

    1. The mutant protein was shown to dimerize in culture cells and retain its MMP inhibitory activity.

      NonPatientCell: ARPE-19 (human retinal pigment epithelial) cell line (CLO:0001749, CL:0009004)

      GeneFunction: GO:0008191 (metalloendopeptidase inhibitor activity), GO:0046872 (metal ion binding), GO:0002020 (protease binding), GO:0005615 (active in extracellular space), GO:0031012 (active in extracellular matrix)

      GeneAlteration: A TIMP3 expression construct encoding the Glu162Lys variant (referred to in the paper as "Glu139Lys") was generated by PCR-based mutagenesis of the wild-type pCDNA3-TIMP3.

      FunctionalEvidence: The TIMP3 variant was exogenously expressed in ARPE-19 cells alongside a mock transfected control (not a wild-type control). Immunoblotting of non-reduced samples detected both monomeric (24 kDa) and dimeric (48 kDa) forms of the variant (Figure 8). Reverse zymographs of extracellular matrix from both wild-type TIMP3- and variant TIMP3-transfected cells revealed the presence of the dimeric species for the variant but not the wild-type, and confirmed its intact metalloproteinase inhibitory activity (Figure 9). This indicated that the free cysteine present in the variant may not have compromised metalloproteinase inhibitory activity, but likely facilitated an intramolecular disfulfide bonding interaction with another TIMP3 molecule. This gain-of-function interpretation of the variant effect would be consistent with the autosomal dominant mechanism of inheritance.

      FAVariants: Variant used was NM_000362.5(TIMP3):c.484G>A (p.Glu162Lys) (CAID:CA411540222). The variant is referred to in this publication as "Glu139Lys" (due to the removal of a 23-amino acid N-terminal signal peptide from the polypeptide sequence) but encodes Glu162Lys in the full/updated polypeptide sequence.

    1. While pluripotent mesenchymal cell lines can be induced into the osteoblastic lineage, they may not reflect endogenous osteoblastic proliferation and differentiation. Consequently, we sought to determine whether the secreted form of LRP5 (LRP5ΔTM) could interfere with bone accrual in calvarial explant cultures. In three independent experiments, explants that were cultured in the presence of conditioned media from cells expressing LRP5ΔTM consistently had thinner bone, as determined by ALP staining and von Kossa staining, than did explants that were cultured in conditioned media from cells expressing wild-type LRP5 (Figure 7). Thus, LRP5ΔTM is able to inhibit bone growth, presumably by binding and interfering with secreted growth factors such as Wnts.

      ExperimentName: LRP5 inhibition using a dominant negative construct blocks bone accrual in mouse calvarial explant culture.

      NonPatientCell: CL:0001035 (bone cell, specifically mouse calvarial explant cultures)

      GeneFunction: GO:0098868 (bone growth)

      GeneAlteration: Calvarial explant cultures from mice were treated with conditioned media from cells exogenously secreting either wild-type LRP5 or dominant negative LRP5deltaTM.

      FunctionalEvidence: Bone accrual / thickness decreases significantly at multiple points in mouse calvarial (skull) explants treated with LRP5deltaTM relative to LRP5-WT (Figure 7).

      FAVariants: LRP5 function was attenuated using an artificial dominant negative mutant while a human variant was not introduced into the LRP5 gene.

    1. OPN1LW gene transcripts expressed in transiently transfected human embryonic kidney (HEK293T) cells. A: Relative expression (RE) levels of unspliced transcripts determined by qPCR across the following boundaries: exon 4 – intron 4; intron 4 – exon 5; exon 5 – intron 5; and intron 5 – exon 6. B: Relative levels of spliced OPN1LW gene transcripts, measured by qPCR, using primer sets that generate amplicons form exon 4 – exon 5 and exon 5 – exon 6. In all cases, the RE values represent OPN1LW mRNA expression normalized to the geometric mean of two internal control genes, RPL13A and EF1A1. Wild-type (WT), black; variant 1 (V1), white; variant 2 (V2), gray; variant 3 (V3), hatched. * and ** denote statistical significance at 1% and 5% probability levels, respectively.

      ExperimentName: OPN1LW variants identified in myopic patients were expressed exogenously in HEK293T cells and exhibited reduced expression at the mRNA level.

      NonPatientCell: HEK293T cells (EFO:0001184)

      GeneFunction: GO:0007602 (phototransduction)

      GeneAlteration: Site-directed mutagenesis was used to introduce the variants into minigenes encoding portions of the wlid-type OPN1LW gene.

      FunctionalEvidence: Three OPN1LW variants identified in myopic patients were expressed exogenously in HEK293T cells and two out of three exhibited reduced expression at the mRNA level (Figures 1A and 1B).

      FAVariants: NM_020061.6(OPN1LW):c.973A>G (p.Met325Val), CA415309107, NM_020061.6(OPN1LW):c.970T>A (p.Phe324Ile), CA415309100, NM_020061.6(OPN1LW):c.971T>A (p.Phe324Tyr), CA415309101

    1. The RetGC1 encoded by the cDNA fragment intended for the transgenic expression in the retina was first tested for Ca2+ sensitivity, apparent affinity for GCAP1, and sensitivity to inhibition by RD3, by being expressed in HEK293 cells under control of a CMV promoter (46.Peshenko I.V. Moiseyev G.P. Olshevskaya E.V. Dizhoor A.M. Factors that determine Ca2+ sensitivity of photoreceptor guanylyl cyclase: kinetic analysis of the interaction between the Ca2+-bound and the Ca2+-free guanylyl cyclase activating proteins (GCAPs) and recombinant photoreceptor guanylyl cyclase 1 (RetGC-1).Biochemistry. 2004; 43: 13796-13804Crossref PubMed Scopus (42) Google Scholar) (Fig. 1). Consistently with the original in vitro observations by Ramamurthy et al. (45.Ramamurthy V. Tucker C. Wilkie S.E. Daggett V. Hunt D.M. Hurley J.B. Interactions within the coiled-coil domain of RetGC-1 guanylyl cyclase are optimized for regulation rather than for high affinity.J. Biol. Chem. 2001; 276: 26218-26229Abstract Full Text Full Text PDF PubMed Scopus (84) Google Scholar), and later by Peshenko et al. (46.Peshenko I.V. Moiseyev G.P. Olshevskaya E.V. Dizhoor A.M. Factors that determine Ca2+ sensitivity of photoreceptor guanylyl cyclase: kinetic analysis of the interaction between the Ca2+-bound and the Ca2+-free guanylyl cyclase activating proteins (GCAPs) and recombinant photoreceptor guanylyl cyclase 1 (RetGC-1).Biochemistry. 2004; 43: 13796-13804Crossref PubMed Scopus (42) Google Scholar), the half-maximal deceleration of the GCAP1-activated cyclase by calcium was shifted toward nearly 2.5-fold higher concentrations (Fig. 1A). The apparent affinity of the R838S RetGC1 for the Mg2+-liganded activator form of GCAP1 (19.Dizhoor A.M. Olshevskaya E.V. Peshenko I.V. Mg2+/Ca2+ cation binding cycle of guanylyl cyclase activating proteins (GCAPs): role in regulation of photoreceptor guanylyl cyclase.Mol. Cell Biochem. 2010; 334: 117-124Crossref PubMed Scopus (78) Google Scholar) became nearly 5-fold higher than normal (KMgGCAP1 327 ± 10 nm (S.D.) versus 1585 ± 80 nm in wild type) (Fig. 1B). In addition to its being the main reason for less effective deceleration by Ca2+ (44.Tucker C.L. Woodcock S.C. Kelsell R.E. Ramamurthy V. Hunt D.M. Hurley J.B. Biochemical analysis of a dimerization domain mutation in RetGC-1 associated with dominant cone-rod dystrophy.Proc. Natl. Acad. Sci. U.S.A. 1999; 96: 9039-9044Crossref PubMed Scopus (87) Google Scholar, 45.Ramamurthy V. Tucker C. Wilkie S.E. Daggett V. Hunt D.M. Hurley J.B. Interactions within the coiled-coil domain of RetGC-1 guanylyl cyclase are optimized for regulation rather than for high affinity.J. Biol. Chem. 2001; 276: 26218-26229Abstract Full Text Full Text PDF PubMed Scopus (84) Google Scholar46.Peshenko I.V. Moiseyev G.P. Olshevskaya E.V. Dizhoor A.M. Factors that determine Ca2+ sensitivity of photoreceptor guanylyl cyclase: kinetic analysis of the interaction between the Ca2+-bound and the Ca2+-free guanylyl cyclase activating proteins (GCAPs) and recombinant photoreceptor guanylyl cyclase 1 (RetGC-1).Biochemistry. 2004; 43: 13796-13804Crossref PubMed Scopus (42) Google Scholar), observed in Fig. 1A, the higher affinity for GCAP1 proportionally correlated with a reduced sensitivity of the GCAP1-activated RetGC1 to the inhibition by RD3: the K½ RD3 rose from 2.6 ± 1.2 versus 11.4 ± 0.4 nm, respectively (p < 0.01), in the R838S RetGC1 (Fig. 1C).

      ExperimentName: Higher GUCY2D activity in the R838S variant

      NonPatientCell: HEK293 cells (EFO:0001182)

      GeneFunction: GO:0006182 (cGMP biosynthetic process)

      GeneAlteration: Site-directed mutagenesis was used to introduce the substitution encoding the R838S substitution into the gene expression construct (PMID: 15504042).

      FunctionalEvidence: The variant exhibits higher activity than the wild-type in HEK293 cells, with enhanced Ca2+ sensitivity (Figure 1A), higher GCAP1 affinity, (Figure 1B), and reduced sensitivity to RD3 inhibition (Figure 1C).

      FAVariants: NM_000180.4(GUCY2D):c.2512C>A (p.Arg838Ser) (ClinVar: 98568)

    1. We have expressed four SFD mutant TIMP-3 proteins in baby hamster kidney (BHK) cells and evaluated their characteristics alongside wild-type TIMP-3.

      ExperimentName: Functional testing of Ser179Cys, Gly190Cys, Tyr191Cys and Ser204Cys variants of TIMP3 in baby hamster kidney (BHK) cells

      NonPatientCell: Baby hamster kidney (BHK) cells, EFO:0001643 (kidney-derived cell line), CLO:0000696 (immortal hamster kidney-derived cell line), CLO:0001965 (BHK-21 cell line)

      GeneFunction: GO:0008191 (metalloendopeptidase inhibitor activity), GO:0046872 (metal ion binding), GO:0002020 (protease binding), GO:0005615 (active in extracellular space), GO:0031012 (active in extracellular matrix)

      GeneAlteration: TIMP3 expression constructs encoding the Ser179Cys, Gly190Cys, Tyr191Cys, and Ser204Cys variants (referred to in the paper as "Ser156Cys", "Gly167Cys", "Tyr166Cys", and "Ser181Cys") were generated by PCR-based mutagenesis of wild-type TIMP3 and cloned into the pNUT expression vector.

      FunctionalEvidence: BHK cells were stably transfected with each of four variants or wild-type TIMP3. All variants expressed and localized successfully to the extracellular matrix (western blotting), Both variants tested exhibited intact metalloproteinase inhibitor activity in ECM fractions (reverse zymography). All four of the variants accumulated as higher molecular weight species (Figure 1A, Figure 2), with Ser179Cys and Ser204Cys in particular accumulating to a much greater degree than the other variants or the wild-type control (Figure 2). Cell morphology and adherence were affected within the variant-expressing cells. While wild-type-transfected cells were more adherent to the ECM than the untransfected controls were, both variant-transfected cells (Ser179Cys, Ser204Cys) were even more ECM-adherent (Figure 5). Association constants were measured for TIMP3 interaction with a series of metalloproteinases, calculating their values for wild-type TIMP3 and for the Ser156Cys variant, which exhibited a 2- or 3-fold loss of reduction, depending on the substrate (Table 2).

      FAVariants: The four variants used were NM_000362.5(TIMP3):c.536C>G, p.Ser179Cys (ClinVar:12678), NM_000362.5(TIMP3):c.568G>T, p.Gly190Cys (CA411540415), NM_000362.5(TIMP3):c.572A>G, p.Tyr191Cys (ClinVar:12677), and NM_000362.5(TIMP3):c.610A>T, p.Ser204Cys (ClinVar:12676).

    1. Blocking the action of CD44 and IMPG1 in pluripotent stem cell derived retinal organoids affected the development of photoreceptors, their inner/outer segments and connecting cilia and disrupted IPM formation, with IMPG1 having an earlier and more significant impact. Together, our data suggest an important role for IMPG1 and CD44 in the development of photoreceptors and IPM formation during human retinogenesis.

      ExperimentName: Blocking IMPG1 in retinal organoids disrupts early development of IPM, photoreceptors and inner/outer segments, and connecting cilia.

      NonPatientCell: UBERON:0000966 (retina, specifically IPSC-derived retinal organoids) or CL:0009004 (retinal cell)

      GeneFunction: GO:0033165 (interphotoreceptor matrix)

      GeneAlteration: Alteration was not performed at the genetic level, but rather a blocking antibody to IMPG1 protein was added to the culture media of the developing retinal organoid at days 90 and 150 of the differentiation process. After incubation, the effects were assessed by IHC and qRT-PCR detecting key markers of differentiation (Figure 6, Figures S12-S15).

      FunctionalEvidence: Expression of RCVRN (a marker of photoreceptor and bipolar cells) and proportion of recoverin-positive cells were reduced (Figs. 6B, S12B, S14B, S14C, S15B). Expression of ARL13B (marker of photoreceptor connecting cilia) was reduced (Figs. 6B, S15B). Expression of RBP3 (marker of IPM formation) was changed only at the later time point (Figs. 6B, S12B, S15B). Expression of OPN1LW/OPN1MW (cone marker) was down-regulated (Fig. S14B). Expression of RHO (rod cell marker) and proportion of rhodopsin-positive cells were reduced, and the typical pattern of staining was replaced with a punctate pattern at the surface of the organoids (Fig. 6B, 6C). Staining for WGA (rod inner/outer segment marker) was reduced, indicating disrupted development of these structures (Fig. 6B, 6C). The authors conclude that IMPG1 is important for development of photoreceptors, inner and outer segments, connecting cilia, and IPM.

      FAVariants: No variant in IMPG1 was used, but rather an inhibitory antibody.

    1. Results

      NonPatientCell: EFO:0001182 (HEK293 Cells)

      GeneFunction: GO:0008233 (Peptidase activity)

      GeneAlteration: HEK293 cells were grown and 8 missense mutations were identified and generated by PCR-mutagenesis. The human mutant cDNAs were transfected into the cells using the calcuim-phosphate coprecipitation method and examined.

      FunctionalEvidence: When HEK293 cells were transfected with wild-type and mutant human cDNA for PHEX, the resulting cells were subject to immunoblotting to determine the protein levels in both the cell lysate and the media of cells. All the variants and the wild-type showed presence in the lysate at various levels, but C85R, G579R, G579V, S711R, and A720T were all devoid of any secreted protein in the media. Ananlysis of these cells also showed possible rescue by growing transfected cells at 26 C, thus glycosylating and maturing the proteins. The endopeptidase activity of the wild-type and variants were also compared, with D237G and Y317F mutant proteins exhibiting 50–60% of wild-type activity; E581V and S711R also displayed nearly undetectable activity. This displayed that the disease causing mechanism could be related to loss of function of peptidase activity or cellular trafficking. Evidence is found under "Results".

      FAVariant1: NM_000444.5:c.253T>C (p.Cys85Arg)

      ClinVar: 438549 https://www.ncbi.nlm.nih.gov/clinvar/variation/438549/

      FAVariant2: NM_000444.5:c.1735G>A (p.Gly579Arg)

      ClinVar: 226119 https://www.ncbi.nlm.nih.gov/clinvar/variation/226119/

      FAVariant3: NM_000444.5:c.1736G>T (p.Gly579Val)

      ClinVar: 372777 https://www.ncbi.nlm.nih.gov/clinvar/variation/372777/

      FAVariant4: NM_000444.5:c.2131A>C (p.Ser711Arg)

      CAID: CA412575294 https://reg.clinicalgenome.org/redmine/projects/registry/genboree_registry/by_caid?caid=CA412575294

      FAVariant5: NM_000444.5:c.2158G>A (p.Ala720Thr)

      CAID: CA412575364 https://reg.clinicalgenome.org/redmine/projects/registry/genboree_registry/by_caid?caid=CA412575364

    2. Results

      NonPatientCell: EFO:0001182 (HEK293 Cells)

      GeneFunction: GO:0008233 (Peptidase activity)

      GeneAlteration: HEK293 cells were grown and 8 missense mutations were identified and generated by PCR-mutagenesis. The human mutant cDNAs were transfected into the cells using the calcuim-phosphate coprecipitation method and examined.

      FunctionalEvidence: When HEK293 cells were transfected with wild-type and mutant human cDNA for PHEX, the resulting cells were subject to immunoblotting to determine the protein levels in both the cell lysate and the media of cells. All the variants and the wild-type showed presence in the lysate at various levels, but C85R, G579R, G579V, S711R, and A720T were all devoid of any secreted protein in the media. Ananlysis of these cells also showed possible rescue by growing transfected cells at 26 C, thus glycosylating and maturing the proteins. The endopeptidase activity of the wild-type and variants were also compared, with D237G and Y317F mutant proteins exhibiting 50–60% of wild-type activity; E581V and S711R also displayed nearly undetectable activity. This displayed that the disease causing mechanism could be related to loss of function of peptidase activity or cellular trafficking. Evidence is found under "Results".

      FAVariant1: NM_000444.5:c.253T>C (p.Cys85Arg)

      ClinVar: 438549 https://www.ncbi.nlm.nih.gov/clinvar/variation/438549/

      FAVariant2: NM_000444.5:c.1735G>A (p.Gly579Arg)

      ClinVar: 226119 https://www.ncbi.nlm.nih.gov/clinvar/variation/226119/

      FAVariant3: NM_000444.5:c.1736G>T (p.Gly579Val)

      ClinVar: 372777 https://www.ncbi.nlm.nih.gov/clinvar/variation/372777/

      FAVariant4: NM_000444.5:c.2131A>C (p.Ser711Arg)

      CAID: CA412575294 https://reg.clinicalgenome.org/redmine/projects/registry/genboree_registry/by_caid?caid=CA412575294

      FAVariant5: NM_000444.5:c.2158G>A (p.Ala720Thr)

      CAID: CA412575364 https://reg.clinicalgenome.org/redmine/projects/registry/genboree_registry/by_caid?caid=CA412575364

    1. Figure 1

      NonPatientCell UBERON:0005424

      GOterm GO:0042802

      GeneAlteration shRNAs cloned into pCAG-mir30 vector that contained a puromycin resistance gene.

      FunctionalEvidence electron microscopy of RPE in 1-2 yo mice showed 37-48% reduced phagocytosis in mutants. (fig. 1) Assayed cryosection of mouse RPE showed mislocalization of adhesion/phagocytosis markers in RPE (fig. 4)

      FAVariants NM_004698.3(PRPF3):c.1481C>T (p.Thr494Met), 3352

    2. Figure 1

      NonPatientCell UBERON:0005424

      GOterm GO:0042802

      GeneAlteration shRNAs cloned into pCAG-mir30 vector that contained a puromycin resistance gene.

      FunctionalEvidence electron microscopy of RPE in 1-2 yo mice showed 37-48% reduced phagocytosis in mutants. (fig. 1) Assayed cryosection of mouse RPE showed mislocalization of adhesion/phagocytosis markers in RPE (fig. 4)

      FAVariants NM_004698.3(PRPF3):c.1481C>T (p.Thr494Met), 3352

    1. Mucopolysaccharidosis type IVA. N-acetylgalactosamine-6-sulfate sulfatase exonic point mutations in classical Morquio and mild cases.

      PMID: 1522213

      Gene: GALNS

      Disease: Mucopolysaccharidosis IVA

      MonDO: MONDO:0009659

      InheritancePattern: AR

      ExperimentName: Expression of variant carrying cDNA in GALNS deficient fibroblasts

      FunctionalEvidence: cDNA encoding each of the 15 variants identified in the study were transfected into a GALNS deficient fibroblast cell line. 14 of the 15 altered cDNA's showed no increase in GALNS activity when the cells were assayed, confirming a lack of enzymatic activity.

      HGNC:

      GeneEvidence:

      SharedGeneImplication:

    2. Mucopolysaccharidosis type IVA. N-acetylgalactosamine-6-sulfate sulfatase exonic point mutations in classical Morquio and mild cases.

      PMID: 1522213

      Gene: GALNS

      Disease: Mucopolysaccharidosis IVA

      MonDO: MONDO:0009659

      InheritancePattern: AR

      ExperimentName: Expression of variant carrying cDNA in GALNS deficient fibroblasts

      FunctionalEvidence: cDNA encoding each of the 15 variants identified in the study were transfected into a GALNS deficient fibroblast cell line. 14 of the 15 altered cDNA's showed no increase in GALNS activity when the cells were assayed, confirming a lack of enzymatic activity.

      HGNC:

      GeneEvidence:

      SharedGeneImplication:

    1. human mononuclear myoblasts

      CellLine: Human Mononuclear Myoblast

      CellEFO: CL:0000056

      GeneFunction: GO:0007015 (Actin Filament Organization)

      GeneAlteration: A wild-type C-terminal EGFP-tagged β-TM fusion gene was generated by amplifying TPM2 and cloning it into a vector while introducing XhoI and EcoRI restriction sites. All mutant constructs were formed by site-directed mutagenesis and cloning into E. coli. These constructs were sequenced to verify the correct coding sequence and introduction of the mutations. They were then introduced to human myoblast cells and mouse C2C12 cells via transfection.

      FunctionalEvidence: The expression of these TPM2 mutants in cultured cells demonstrated several morphological abnormalities reminiscent of those seen in nemaline myopathy patients. In the human myoblasts/differentiated cells, these included various types of aggregates including nuclear, cytoplasmic, endogenous, and perinuclear. Large accumulations of actin along with clouds around the nucleus and cytoplasm with unorganized structure were also present. Poor incorporation of stress fibers, what appeared to be disorganized sarcomeric structure, and rod-like structures both intranuclear and in the myotubes in particular all demonstrate clear similarities to those phenotypes seen in nemaline myopathy, namely the presence of nemaline rods, disorganized sarcomeres, and z-disc abnormalities. These two groups of pathologies also seem to share the same mechanism, specifically the TPM2 mutations destabilizing the actin-myosin structures and causing accumulation and abnormal structures to form. Similarly, the modified C2C12 myoblasts/myotubes also displayed peripheral and perinuclear aggregates in both stages of development as well as diffuse cytoplasmic labeling of stress fibers. They had difficulty differentiating, as they appeared to be fused rather than elongated and multinucleated. This further supports the connection between the gene disruption and the pathologies that are demonstrated here.

      CellVariant1: NM_003289.3:c.121G>A (p.Glu41Lys)

      ClinVar: 12464 http://www.ncbi.nlm.nih.gov/clinvar/variation/12464

      CellVariant2: NM_003289.3:c.142_144delAAG (p.Lys49del)

      ClinVar: 12466 https://www.ncbi.nlm.nih.gov/clinvar/variation/12466/

      CellVariant3: NM_003289.3:c.154_156dup (p.Gly52dup)

      ClinVar: 140485 https://www.ncbi.nlm.nih.gov/clinvar/variation/140485/

      CellVariant4: NM_003289.3:c.364G>A (p.Glu122Lys)

      CAID: CA373367963 http://reg.genome.network/redmine/projects/registry/genboree_registry/by_caid?caid=CA373367963

      CellVariant5: NM_003289.3:c.606C>G (p.Asn202Lys)

      ClinVar: 12467 https://www.ncbi.nlm.nih.gov/clinvar/variation/12467/

    2. human mononuclear myoblasts

      CellLine: Human Mononuclear Myoblast

      CellEFO: CL:0000056

      GeneFunction: GO:0007015 (Actin Filament Organization)

      GeneAlteration: A wild-type C-terminal EGFP-tagged β-TM fusion gene was generated by amplifying TPM2 and cloning it into a vector while introducing XhoI and EcoRI restriction sites. All mutant constructs were formed by site-directed mutagenesis and cloning into E. coli. These constructs were sequenced to verify the correct coding sequence and introduction of the mutations. They were then introduced to human myoblast cells and mouse C2C12 cells via transfection.

      FunctionalEvidence: The expression of these TPM2 mutants in cultured cells demonstrated several morphological abnormalities reminiscent of those seen in nemaline myopathy patients. In the human myoblasts/differentiated cells, these included various types of aggregates including nuclear, cytoplasmic, endogenous, and perinuclear. Large accumulations of actin along with clouds around the nucleus and cytoplasm with unorganized structure were also present. Poor incorporation of stress fibers, what appeared to be disorganized sarcomeric structure, and rod-like structures both intranuclear and in the myotubes in particular all demonstrate clear similarities to those phenotypes seen in nemaline myopathy, namely the presence of nemaline rods, disorganized sarcomeres, and z-disc abnormalities. These two groups of pathologies also seem to share the same mechanism, specifically the TPM2 mutations destabilizing the actin-myosin structures and causing accumulation and abnormal structures to form. Similarly, the modified C2C12 myoblasts/myotubes also displayed peripheral and perinuclear aggregates in both stages of development as well as diffuse cytoplasmic labeling of stress fibers. They had difficulty differentiating, as they appeared to be fused rather than elongated and multinucleated. This further supports the connection between the gene disruption and the pathologies that are demonstrated here.

      CellVariant1: NM_003289.3:c.121G>A (p.Glu41Lys)

      ClinVar: 12464 http://www.ncbi.nlm.nih.gov/clinvar/variation/12464

      CellVariant2: NM_003289.3:c.142_144delAAG (p.Lys49del)

      ClinVar: 12466 https://www.ncbi.nlm.nih.gov/clinvar/variation/12466/

      CellVariant3: NM_003289.3:c.154_156dup (p.Gly52dup)

      ClinVar: 140485 https://www.ncbi.nlm.nih.gov/clinvar/variation/140485/

      CellVariant4: NM_003289.3:c.364G>A (p.Glu122Lys)

      CAID: CA373367963 http://reg.genome.network/redmine/projects/registry/genboree_registry/by_caid?caid=CA373367963

      CellVariant5: NM_003289.3:c.606C>G (p.Asn202Lys)

      ClinVar: 12467 https://www.ncbi.nlm.nih.gov/clinvar/variation/12467/

    1. Apoptosis assay

      PatientCell: CL:0000187 (Muscle Cell)

      GeneFunction: Muscle Cell Apoptotic Process (GO:0010657)

      GeneAlteration: Samples were collected from deltoid muscle biopsy of control individuals and LGMD2C individuals with the 525delT founder mutation. No further alteration necessary.

      FunctionalEvidence: TUNEL staining was perfomed on muscle samples from LGMD2C patients and healthy controls to test for cell apoptosis. No positive staining was detected in any control individuals while it was commonly found in the patient muscle. This indicates that a result of SGCG disruption is increased cellular apoptosis likely contributing to the myofiber degeration and muscle atrophy seen commonly in LGMD patients.

      FAVariant: NM_000231.2(SGCG):c.525del (p.Phe175fs)

      ClinVarID: 189243 https://www.ncbi.nlm.nih.gov/clinvar/variation/189243/

    2. Apoptosis assay

      PatientCell: CL:0000187 (Muscle Cell)

      GeneFunction: Muscle Cell Apoptotic Process (GO:0010657)

      GeneAlteration: Samples were collected from deltoid muscle biopsy of control individuals and LGMD2C individuals with the 525delT founder mutation. No further alteration necessary.

      FunctionalEvidence: TUNEL staining was perfomed on muscle samples from LGMD2C patients and healthy controls to test for cell apoptosis. No positive staining was detected in any control individuals while it was commonly found in the patient muscle. This indicates that a result of SGCG disruption is increased cellular apoptosis likely contributing to the myofiber degeration and muscle atrophy seen commonly in LGMD patients.

      FAVariant: NM_000231.2(SGCG):c.525del (p.Phe175fs)

      ClinVarID: 189243 https://www.ncbi.nlm.nih.gov/clinvar/variation/189243/

    1. Fig. 2

      NonPatientCell Mouse cell line, EFO:0002887 "Myotubes generated from the homozygous dysgenic (mdg/mdg) mouse cell line GLT were cultured as described previously (44)."

      GeneAlteration GFP tagged point mutation transfected into mouse cells

      FunctionalEvidence Variant increased channel sensitivity to caffeine/voltage (fig. 2)

      FAVariants NM_000069.2(CACNA1S):c.3257G>A (p.Arg1086His), ClinVar ID: 17626

      NM_000445.4(PLEC):c.3719G>A (p.Arg1240His), ClinVar ID: 448061

    2. Fig. 2

      NonPatientCell Mouse cell line, EFO:0002887 "Myotubes generated from the homozygous dysgenic (mdg/mdg) mouse cell line GLT were cultured as described previously (44)."

      GeneAlteration GFP tagged point mutation transfected into mouse cells

      FunctionalEvidence Variant increased channel sensitivity to caffeine/voltage (fig. 2)

      FAVariants NM_000069.2(CACNA1S):c.3257G>A (p.Arg1086His), ClinVar ID: 17626

      NM_000445.4(PLEC):c.3719G>A (p.Arg1240His), ClinVar ID: 448061

    1. Figure 2

      PatientCell CL:0000057 (fibroblast)

      GeneFunction GO:0070131 (positive regulation of mitochondrial translation)

      GeneAlteration n/a

      FunctionalEvidence (Figure 2D) Labelling patient fibroblast proteins with EasyTag EXPRESS35S Protein Labeling Mix showed decreased assembly of complex I (NDUFB8) and IV (COXI) which corroborates the reduced mean enzyme activity and mitochondrial translation in Table 1.

      FAVariants NM_017819.3(TRMT10C):c.814A>G (p.Thr272Ala)

      ClinVar: 224317

      and

      NM_017819.3(TRMT10C):c.542G>T (p.Arg181Leu)

      ClinVar: 224316

    2. Figure 2

      PatientCell CL:0000057 (fibroblast)

      GeneFunction GO:0070131 (positive regulation of mitochondrial translation)

      GeneAlteration n/a

      FunctionalEvidence (Figure 2D) Labelling patient fibroblast proteins with EasyTag EXPRESS35S Protein Labeling Mix showed decreased assembly of complex I (NDUFB8) and IV (COXI) which corroborates the reduced mean enzyme activity and mitochondrial translation in Table 1.

      FAVariants NM_017819.3(TRMT10C):c.814A>G (p.Thr272Ala)

      ClinVar: 224317

      and

      NM_017819.3(TRMT10C):c.542G>T (p.Arg181Leu)

      ClinVar: 224316