| Version | Summary | Created by | Modification | Content Size | Created at | Operation |
|---|---|---|---|---|---|---|
| 1 | Camila Xu | -- | 1395 | 2022-11-02 01:32:44 |
Glycogen synthase, an enzyme that is responsible in glycogen synthesis, is activated by glucose 6-phosphate (G6P), and inhibited by glycogen synthase kinases (GSK3). Those two mechanisms play an important role in glycogen metabolism. Glycogen synthase kinase (GSK-3) is a serine/threonine kinase that phosphorylate either threonine or serine, and this phosphorylation permits a variety of biological activities as glycogen metabolism, cell signaling, cellular transport, and others. GS inhibition by GSK-3β leads to a decrease in glycogen synthesis in the liver and muscles, along with increased blood glucose or hyperglycemia. This is why GSK-3β is associated with the pathogenesis and progression of many diseases, such as diabetes, obesity, and cancer. Human GSK-3 has two isoforms, α and β. It is active in resting cells and is inhibited by several hormones such as insulin, endothelial growth factor, and platelet-derived growth factor. Insulin inactivates it by phosphorylation of the specific serine residues Ser21 and Ser9 in GSK-3 isoforms α and β, respectively. In a phosphatidylinositol 3-kinase-dependent way. Glycogen synthase kinase inhibitors are different chemotypes and have variable mechanisms of action; they may be cations, from natural sources, synthetic ATP and non-ATP competitive inhibitors and substrate-competitive inhibitors. GSK3 is a bi-lobar architecture with N-terminal and C-terminal, the N-terminal is responsible for ATP binding and C-terminal which is called as activation loop mediates the kinase activity, Tyrosine located at the C-terminal it essential for full GSK3 activity.