Phospho-GSK-3beta (Thr390) Antibody

Glycogen synthase kinase-3 (GSK-3) was initially identified as an enzyme that regulates glycogen synthesis in response to insulin (1). GSK-3 is a ubiquitously expressed serine/threonine protein kinase that phosphorylates and inactivates glycogen synthase. GSK-3 is a critical downstream element of the PI3K/Akt cell survival pathway whose activity can be inhibited by Akt-mediated phosphorylation at Ser21 of GSK-3α and Ser9 of GSK-3β (2,3). GSK-3 has been implicated in the regulation of cell fate in Dictyostelium and is a component of the Wnt signaling pathway required for Drosophila, Xenopus, and mammalian development (4). GSK-3 has been shown to regulate cyclin D1 proteolysis and subcellular localization (5).The phosphorylation of GSK-3β at Thr390 was found to be a possible substrate of p38 MAPK and was reported by several labs using phosphoproteomic analysis on mitotic cell extracts (6-10). Phosphorylation of this site was also identified at Cell Signaling Technology (CST) using PhosphoScan®, CST's LC-MS/MS platform for modification site discovery (11). Please visit PhosphoSitePlus®, CST's modification site knowledgebase, at www.phosphosite.org for more information. 1.Welsh, G.I. et al. (1996) Trends Cell Biol 6, 274-9. 2.Srivastava, A.K. and Pandey, S.K. (1998) Mol Cell Biochem 182, 135-41. 3.Cross, D.A. et al. (1995) Nature 378, 785-9. 4.Nusse, R. (1997) Cell 89, 321-3. 5.Diehl, J.A. et al. (1998) Genes Dev 12, 3499-511. 6.Thornton, T.M. et al. (2008) Science 320, 667-70. 7.Daub, H. et al. (2008) Mol Cell 31, 438-48. 8.Dephoure, N. et al. (2008) Proc Natl Acad Sci USA 105, 10762-7. 9.Lowery, D.M. et al. (2007) EMBO J 26, 2262-73. 10.Beausoleil, S.A. et al. (2004) Proc Natl Acad Sci USA 101, 12130-5. 11.Rush, J. et al. (2005) Nat Biotechnol 23, 94-101.