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The complex formation of PKCdelta through its C1- and C2-like regions in H2O2-stimulated cells.

Abstract：

:PKCdelta was revealed to make a homologous protein complex that shows a high protein kinase activity upon H(2)O(2) stimulation by expressing the enzymes having different epitope tags in COS-7 cells. The association of the endogenous PKCdelta in the cells was observed by sucrose density gradients. Analysis using the mutant replacing the tyrosine phosphorylation sites showed that PKCdelta is activated without tyrosine phosphorylation in the stimulated cells, and the time course of the activation was parallel with that of the complex formation. The binding sites were identified as the C1 and C2-like regions in the regulatory domain using a series of deletion mutants. The binding between the C1 and C2-like region fragments was induced by cell stimulation, whereas the association of the C1 region fragments by itself and that of the C2-like region fragments were observed even without stimulation. These results suggest that the protein complexes of PKCdelta through the association between the C1 and C2-like regions by different combinations are generated in the H(2)O(2)-treated cells, that may show an enhanced protein kinase activity.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Umada-Kajimoto S,Yamamoto T,Matsuzaki H,Kikkawa U

doi

10.1016/j.bbrc.2005.12.161

subject

Has Abstract

pub_date

2006-03-03 00:00:00

pages

101-7

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(05)02944-X

journal_volume

341

pub_type

杂志文章

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