Phosphorylation and inactivation of glycogen synthase kinase 3 by protein kinase A
نویسندگان
چکیده
منابع مشابه
Phosphorylation and inactivation of glycogen synthase kinase 3 by protein kinase A.
Glycogen synthase kinase 3 (GSK-3) is implicated in multiple biological processes including metabolism, gene expression, cell fate determination, proliferation, and survival. GSK-3 activity is inhibited through phosphorylation of serine 21 in GSK-3 alpha and serine 9 in GSK-3 beta. These serine residues of GSK-3 have been previously identified as targets of protein kinase B (PKB/Akt), a serine/...
متن کاملPhosphorylation and inactivation of glycogen synthase by phosphorylase kinase.
Skeletal muscle glycogen a4-synthase (EC 2.4.1.11) has been purified free of all synthase kinase and phosphatase activities by chromatography on a Glc-N-6-P-Sepharose affinity column and then on a phosphocellulose column. This preparation of glycogen synthase was tested as a substrate for purified skeletal muscle phosphorylase kinase (ATP:phosphorylase-b phosphotransferase, EC 2.7.1.38). Phosph...
متن کاملGlycogen Synthase Kinase-3
1Department of Pathology and Centre for Neuroscience, The University of Melbourne and Mental Health Research Institute, Parkville, VIC 3010, Australia 2Neurosignalling Group, Garvan Institute for Medical Research, 384 Victoria St. Darlinghurst, Sydney, NSW 2010, Australia 3Membrane Biology Group, Centre for Integrative Physiology, University of Edinburgh, George Square, Edinburgh EH8 9XD, UK 4 ...
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Tau is primarily a neuronal microtubule-associated protein that has functions related to the stabilisation of microtubules. Phosphorylation of tau is an important dynamic and regulatory element involved in the binding of tau to tubulin. Thus, highly phosphorylated tau is more likely to be present in the cytosolic compartment of neurons, whereas reduced phosphate burden allows tau to bind to and...
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Glycogen synthase kinase-3 (GSK-3), a protein-serine kinase implicated in cell-fate determination and differentiation, phosphorylates several regulatory proteins that are activated by dephosphorylation in response to hormones or growth factors. GSK-3 beta is phosphorylated in vitro at serine 9 by p70 S6 kinase and p90rsk-1, resulting in its inhibition [Sutherland, Leighton, and Cohen (1993) Bio...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 2000
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.220413597