Phosphorylation by p38 MAPK as an alternative pathway for GSK3beta inactivation.
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ABSTRACT:
SUBMITTER: Thornton TM
PROVIDER: S-EPMC2597039 | biostudies-literature | 2008 May
REPOSITORIES: biostudies-literature
Publications
Phosphorylation by p38 MAPK as an alternative pathway for GSK3beta inactivation.
Thornton Tina M TM Pedraza-Alva Gustavo G Deng Bin B Wood C David CD Aronshtam Alexander A Clements James L JL Sabio Guadalupe G Davis Roger J RJ Matthews Dwight E DE Doble Bradley B Rincon Mercedes M
Science (New York, N.Y.) 20080501 5876
Glycogen synthase kinase 3beta (GSK3beta) is involved in metabolism, neurodegeneration, and cancer. Inhibition of GSK3beta activity is the primary mechanism that regulates this widely expressed active kinase. Although the protein kinase Akt inhibits GSK3beta by phosphorylation at the N terminus, preventing Akt-mediated phosphorylation does not affect the cell-survival pathway activated through the GSK3beta substrate beta-catenin. Here, we show that p38 mitogen-activated protein kinase (MAPK) als ...[more]
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