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Differential regulation of glycogen synthase kinase-3 beta by protein kinase C isotypes.
Open accessAbstract
In cells, stimulation of protein kinase C (PKC) results in the dephosphorylation of specific residues proximal to the DNA binding domain of c-Jun, a major component of the AP-1 transcription factor. Since phosphorylation of this region of c-Jun inhibits interaction with DNA, this pathway may contribute to PKC activation of AP-1. To determine the mechanism(s) underlying this pathway, possible interactions between PKC and proteins implicated in c-Jun regulation are being investigated. Here it is shown that glycogen synthase kinase-3 beta (GSK-3 beta), a serine/threonine kinase that specifically targets the inhibitory c-Jun phosphorylation sites, is phosphorylated in vitro by particular forms of PKC (alpha, beta 1, gamma greater than beta 2; not epsilon). By contrast, the related GSK-3 alpha is not a substrate for any of these PKC isotypes. Phosphorylation of GSK-3 beta by PKC results in its specific inactivation. These results are consistent with a model in which activation of PKC stimulates c-Jun DNA binding by inhibiting its phosphorylation by GSK-3 beta.
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Metadata
- Authors
- Goode, N., Hughes, K., Woodgett, J. R., & Parker, P. J.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1992-10
- Volume
- 267
- Issue
- 24
- Pages
- 16878-16882
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1758789982
- Cited by
- 396
- References
- 0
- FWCI
- 4.58
- Type
- journal article
- Language
- en
- Open access
- hybrid
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