On 2015 Aug 12, Jim Woodgett commented:

This manuscript would be improved by systematic removal of "beta" throughout as the inhibitor primarily used, GIN, is not selective for GSK-3beta vs the related isoform, GSK-3alpha. A direct quote from reference 17 (referring to the source of the GIN inhibitor used here):

"A similar assay measuring inhibition of GSK3-alpha was also routinely run, but 7-12 showed no significant ability to discriminate between the two isoforms of GSK3 (data not shown). To the best of our knowledge, no isoform specific inhibitors of GSK3 have been reported, probably due to their high sequence homology (vida supra)."

This inhibitor (GIN) acts equally on both isoforms of GSK-3 (alpha and beta) and should not be referred to as a GSK-3beta selective inhibitor. This makes sense given that inhibition of GSK-3beta alone is insufficient for deregulation of beta-catenin (PMID: 17543867).

On 2015 Aug 12, Jim Woodgett commented:

This manuscript would be improved by systematic removal of "beta" throughout as the inhibitor primarily used, GIN, is not selective for GSK-3beta vs the related isoform, GSK-3alpha. A direct quote from reference 17 (referring to the source of the GIN inhibitor used here):

"A similar assay measuring inhibition of GSK3-alpha was also routinely run, but 7-12 showed no significant ability to discriminate between the two isoforms of GSK3 (data not shown). To the best of our knowledge, no isoform specific inhibitors of GSK3 have been reported, probably due to their high sequence homology (vida supra)."

This inhibitor (GIN) acts equally on both isoforms of GSK-3 (alpha and beta) and should not be referred to as a GSK-3beta selective inhibitor. This makes sense given that inhibition of GSK-3beta alone is insufficient for deregulation of beta-catenin (PMID: 17543867).