GSK-3 alpha/beta Products

Description

Glycogen Synthase Kinase 3beta (GSK-3beta) is a unique serine/threonine kinase that is inactivated by phosphorylation. In response to insulin binding, PKB/AKT phosphorylates GSK-3beta on serine 9, which prevents GSK-3beta from phosphorylating glycogen synthase. Unphosphorylated glycogen synthase is active and able to synthesize glycogen. GSK-3beta is also unique in that it requires a substrate that has been phosphorylated by a distinct kinase before it can phosphorylate the substrate. This phosphate priming mechanism explains why phosphorylation of serine 9 inactivates GSK-3beta. The phosphorylated serine binds to the GSK-3beta priming phosphate position and prevents binding of alternative substrates. In addition to insulin signaling, GSK-3beta participates in the Wnt signaling pathway, where it forms a complex with axin, beta-catenin and adenomatous polyposis coli (APC) protein. In the presence of Wnts, GSK-3beta is unable to phosphorylate beta-catenin, which leads to stabilization of beta-catenin. The Wnt pathway inactivates GSK-3beta via the proteins, Dishevelled and FRAT, which disrupt the interaction of GSK-3beta with axin, beta-catenin, and APC. Clinically, there is considerable interest in GSK-3beta inhibitors because they may mimic the effect of insulin or reduce the hyperphosphorylation of Tau that is observed in Alzheimer's Disease.

Bioinformatics

Entrez	2931 Human 2932 Human 50686 Rat 606496 Mouse
Uniprot	P18266 Rat P49840 Human
Product By Gene ID	2931
Alternate Names	DKFZp686D0638 EC 2.7.11 EC 2.7.11.26 glycogen synthase kinase 3 alpha glycogen synthase kinase-3 alpha GSK-3 alpha

Research Areas for GSK-3 alpha/beta

Find related products by research area and learn more about each of the different research areas below.

Cell Biology
Hypoxia
Phospho-Specific
Protein Kinase
Signal Transduction
Stem Cell Markers