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

Abstract：

: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.

journal_name

Proc Natl Acad Sci U S A

journal_title

Proceedings of the National Academy of Sciences of the United States of America

authors

Fang X,Yu SX,Lu Y,Bast RC Jr,Woodgett JR,Mills GB

doi

10.1073/pnas.220413597

keywords:

subject

Has Abstract

pub_date

2000-10-24 00:00:00

pages

11960-5

issue

22

eissn

0027-8424

issn

1091-6490

pii

220413597

journal_volume

97

pub_type

杂志文章

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