Glycogen synthase kinase-3 beta is a dual specificity kinase differentially regulated by tyrosine and serine/threonine phosphorylation.
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چکیده
منابع مشابه
Glycogen synthase kinase 3- and extracellular signal-regulated kinase-dependent phosphorylation of paxillin regulates cytoskeletal rearrangement.
Paxillin is a 68-kDa focal adhesion-associated protein that plays an important role in controlling cell spreading and migration. Phosphorylation of paxillin regulates its biological activity and thus has warranted investigation. Serine 126 and serine 130 were previously identified as two major extracellular signal-regulated kinase (ERK)-dependent phosphorylation sites in Raf-transformed fibrobl...
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Kinases can phosphorylate and regulate androgen receptor activity during prostate cancer progression. In particular, we showed that glycogen synthase kinase-3 beta phosphorylates the androgen receptor, thereby inhibiting androgen receptor-driven transcription. Conversely, the glycogen synthase kinase-3 beta inhibitor lithium chloride suppressed the glycogen synthase kinase-3 beta-mediated phosp...
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 ...
متن کاملGlycogen Synthase Kinase 3 Is a Natural Activator of Mitogen-activated Protein Kinase/Extracellular Signal-regulated
Glycogen synthase kinase 3 (GSK3 ) is implicated in many biological events, including embryonic development, cell differentiation, apoptosis, and insulin response. GSK3 has now been shown to induce activation of the mitogen-activated protein kinase kinase kinase MEKK1 and thereby to promote signaling by the stressactivated protein kinase pathway. GSK3 -binding protein blocked the activation of ...
متن کاملPhosphorylation 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/...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1994
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(17)36661-9