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Mitogen inactivation of glycogen synthase kinase-3 β in intact cells via serine 9 phosphorylation
Open accessAbstract
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.
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Sutherland, C., Leighton, I. A., & Cohen, P. (1993) · Biochemical Journal · doi:10.1042/bj2960015 · Cited by 903
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Metadata
- Authors
- Stambolic, V, & Woodgett, J. R.
- Venue
- Biochemical Journal
- Publisher
- Portland Press Ltd.
- Published
- 1994-11-01
- Volume
- 303
- Issue
- 3
- Pages
- 701-704
- ISSN
- 0264-6021 (ISSN-L)
- 1470-8728
- OpenAlex
- W65155625
- Cited by
- 581
- References
- 1
- FWCI
- 3.43
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Stambolic, V, & Woodgett, J. R. (1994). Mitogen inactivation of glycogen synthase kinase-3 β in intact cells via serine 9 phosphorylation. Biochemical Journal. https://doi.org/10.1042/bj3030701
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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