Differential regulation of glycogen synthase kinase-3 beta by protein kinase C isotypes.

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.
Mesh Terms:
Calcium-Calmodulin-Dependent Protein Kinases, Cell Line, Genes, jun, Glycogen Synthase Kinases, Hela Cells, Homeostasis, Humans, Isoenzymes, Models, Biological, Muscles, Peptide Mapping, Phosphopeptides, Phosphorylation, Protein Kinase C, Protein Kinases, Proto-Oncogene Proteins c-jun, Recombinant Proteins
J. Biol. Chem.
Date: Aug. 25, 1992
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