p-GSK-3α/β Antibody (6D3): sc-81496

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Glycogen synthase kinase-3å (GSK-3å) and GSK-3∫ are highly similar isoforms of serine/ threonine kinases that regulate metabolic enzymes and transcription factors, which are responsible for coordinating processes such as glycogen synthesis and cell adhesion. GSK-3∫ activity is also required for nuclear activity of Rel dimers, which mediate an anti-apoptotic response to TNFå in mice. GSK-3 catalytic kinase activity is controlled through differential phosphorylation of serine/threonine residues, which have an inhibitory effect, and tyrosine residues, which have an activating effect. Growth factor stimulation of mammalian cells expressing GSK-3å and GSK-3∫ induces phosphorylation of Ser 21 and Ser 9, respectively, through a phosphatidylinositol 3-kinase (PI 3-K)-protein kinase B (PKB)-dependent pathway, thereby enhancing proliferative signals. Additionally, GSK-3 physically associates with cAMP-dependent protein kinase A (PKA), which phosphorylates Ser 21 of GSK-3å or Ser 9 of GSK-3∫ and inactivates both forms. GSK-3å/∫ is positively regulated by phosphorylation on Tyr 279 and Tyr 216, respectively. Activated GSK-3å/∫ participates in energy metabolism, neuronal cell development, and body pattern formation. Tyrosine dephosphorylation of GSK-3 is involved in its extracellular signal-dependent inactivation.