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Mitogen inactivation of glycogen synthase kinase-3 beta in intact cells via serine 9 phosphorylation.

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) Biochem. J. 296, 15-19]. Using HeLa cells expressing GSK-3 beta or a mutant containing alanine at residue 9, we demonstrate that serine 9 is modified in intact cells and is targeted specifically by p90rsk-1, and that phosphorylation leads to loss of activity. Since p90rsk-1 is directly activated by mitogen-activated protein kinases, agonists of this pathway, such as insulin, repress GSK-3 function.

Pubmed ID: 7980435

Authors

  • Stambolic V
  • Woodgett JR

Journal

The Biochemical journal

Publication Data

November 1, 1994

Associated Grants

None

Mesh Terms

  • Amino Acid Sequence
  • Calcium-Calmodulin-Dependent Protein Kinases
  • Glycogen Synthase Kinase 3
  • Glycogen Synthase Kinases
  • HeLa Cells
  • Humans
  • Mitogens
  • Molecular Sequence Data
  • Phosphorylation
  • Point Mutation
  • Serine