RGD Reference Report - Phosphorylation and inactivation of glycogen synthase kinase 3 by protein kinase A. - Rat Genome Database

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Phosphorylation and inactivation of glycogen synthase kinase 3 by protein kinase A.

Authors: Fang, X  Yu, SX  Lu, Y  Bast RC, JR  Woodgett, JR  Mills, GB 
Citation: Fang X, etal., Proc Natl Acad Sci U S A. 2000 Oct 24;97(22):11960-5.
RGD ID: 8554447
Pubmed: PMID:11035810   (View Abstract at PubMed)
PMCID: PMC17277   (View Article at PubMed Central)
DOI: DOI:10.1073/pnas.220413597   (Journal Full-text)

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/threonine kinase located downstream of phosphatidylinositol 3-kinase. Here, we show that serine 21 in GSK-3 alpha and serine 9 in GSK-3 beta are also physiological substrates of cAMP-dependent protein kinase A. Protein kinase A physically associates with, phosphorylates, and inactivates both isoforms of GSK-3. The results indicate that depending on the stimulatory context, the activity of GSK-3 can be modulated either by growth factors that work through the phosphatidylinositol 3-kinase-protein kinase B cascade or by hormonal stimulation of G protein-coupled receptors that link to changes in intracellular cAMP levels.

Gene Ontology Annotations    Click to see Annotation Detail View

Molecular Function

Objects Annotated

Genes (Rattus norvegicus)
Gsk3a  (glycogen synthase kinase 3 alpha)
Gsk3b  (glycogen synthase kinase 3 beta)
Prkaca  (protein kinase cAMP-activated catalytic subunit alpha)


Additional Information