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. 1992 Apr 15;283(Pt 2):515–518. doi: 10.1042/bj2830515

Studies on the phosphorylation of protein kinase C-alpha.

C Pears 1, S Stabel 1, S Cazaubon 1, P J Parker 1
PMCID: PMC1131065  PMID: 1575696

Abstract

A kinase-defective protein kinase C-alpha mutant is shown to be a phosphoprotein when expressed in COS-1 cells, indicating that intramolecular phosphorylation does not fully account for the phosphate content of protein kinase C-alpha. Furthermore, evidence is presented that the intermolecular phosphorylation of protein kinase C-alpha is due to an activity other than protein kinase C-alpha itself, and this phosphorylation appears to be necessary for protein kinase C-alpha activity. By contrast, the characteristic shift in apparent molecular mass consequent on phosphorylation in vivo can be accounted for by autophosphorylation, as demonstrated in vitro. The relationship between these phosphorylated protein kinase C-alpha species is discussed.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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