page_title: GSK-3
hierarchical_section_title: GSK-3
caption_attribution_description: English: Crystallographic structure of human GSK-3β based on 1J1B PDB coordinates (rainbow colored, N-terminus = blue, C-terminus = red).
context_page_description: Glycogen synthase kinase 3 is a serine/threonine protein kinase that mediates the addition of phosphate molecules onto serine and threonine amino acid residues. First discovered in 1980 as a regulatory kinase for its namesake, Glycogen synthase, GSK-3 has since been identified as a kinase for over 100 different proteins in a variety of different pathways. In mammals GSK-3 is encoded by two paralogous genes, GSK-3 alpha and GSK-3 beta. GSK-3 has recently been the subject of much research because it has been implicated in a number of diseases, including Type II diabetes, Alzheimer's disease, inflammation, cancer, and bipolar disorder.
  Glycogen synthase kinase 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, cancer, and Alzheimer's disease.
context_section_description: Glycogen synthase kinase 3 is a serine/threonine protein kinase that mediates the addition of phosphate molecules onto serine and threonine amino acid residues. First discovered in 1980 as a regulatory kinase for its namesake, Glycogen synthase, GSK-3 has since been identified as a kinase for over 100 different proteins in a variety of different pathways. In mammals GSK-3 is encoded by two paralogous genes, GSK-3 alpha (GSK3A) and GSK-3 beta (GSK3B). GSK-3 has recently been the subject of much research because it has been implicated in a number of diseases, including Type II diabetes (diabetes mellitus type 2), Alzheimer's disease, inflammation, cancer, and bipolar disorder.
  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, cancer, and Alzheimer's disease. 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.
  As of 2019, GSK-3 is the only type of glycogen synthase kinase named and recognized. The gene symbols for GSK1 and GSK2 have been withdrawn by the HUGO Gene Nomenclature Committee (HGNC), and no new names for these "genes" nor their locations have been specified.
caption: Crystallographic structure of human GSK-3β (rainbow colored, N-terminus = blue, C-terminus = red) bound to phosphoaminophosphonic acid-adenylate ester (spheres).[1]
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