Subsequently, two separate isoforms were cloned, termed GSK3α and GSK3β [ … GSK-3 has recently been the subject of much research becaus… The enzyme also cleaves the ester bond between the C1 position of glucose and the pyro… Glycogen synthase (GS) responsible for glycogenesis is the primary substrate of glycogen synthase kinase (GSK)3β and is inactivated by phosphorylation of … In mammals GSK-3 is encoded by two paralogous genes, GSK-3 alpha (GSK3A) and GSK-3 beta (GSK3B). 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. Glycogen synthase kinase 3 (GSK3) was identified over 20 years ago as a protein kinase that phosphorylated and inhibited glycogen synthase [1 ], the enzyme that catalyzes the transfer of glucose from UDPG to glycogen. We report here use of human myoblasts in culture to study the relationships between cellular glycogen concentrations and the activities of glycogen synthase (GS) and AMP-activated protein kinase (AMPK). Incubation of cells for 2 h in the absence of glucose led to a 25% decrease in glycogen content and a significant decrease in the fractional activity of GS. The reaction is highly regulated by allosteric effectors such as glucose 6-phosphate (activator) and by phosphorylation reactions (deactivating). This raises a variety of questions in terms of its physiological role (s), how signaling specificity is maintained and why so many eggs have been placed into one basket. The inactivating phosphorylation is triggered by the hormone glucagon, which is secreted by the pancreas in response to decreased blood glucose levels. Glycogen synthase kinase-3 (GSK-3) is an unusual protein-serine kinase in that it is primarily regulated by inhibition and lies downstream of multiple cell signaling pathways. Glycogen synthase kinase-3 (GSK-3) is a highly conserved negative regulator of receptor tyrosine kinase, cytokine, and Wnt signaling pathways. GSK-3 was originally identified and later embodied as a member of the insulin-signalling pathway responsible for phosphorylation and inactivation of glycogen synthase, a major regulatory enzyme of glycogen metabolism. Glucose-6-phosphate allosteric activating action allows glycogen synthase to operate as a glucose-6-phosphate sensor. Glycogen synthase kinase 3 is a serine/threonine protein kinase that mediates the addition of phosphate molecules onto serine and threonine amino acid residues. Stimulation of these pathways inhibits GSK-3 to modulate diverse downstream effectors that include transcription factors, nutrient sensors, glycogen synthesis, mitochondrial function, circadian rhythm, and cell fate.

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