Protein kinase C forms a complex with and phosphorylates the GTPase activating protein GAP: phosphorylation by PKC is dependent on tyrosine phosphorylation of GAP and/or a GAP-associated protein.

Abstract:

:Protein kinase C (PKC) and the GTPase-activating protein GAP can be detected in immunoprecipitates of mouse epidermis and lung cytosol obtained with either anti-GAP or anti-PKC antisera. The PKC in the immune-complex phosphorylates the coprecipitated GAP protein. Moreover, purified recombinant GAP is phosphorylated in vitro by purified PKC. The efficacy of this phosphorylation appears to depend on the extent of tyrosine phosphorylation of GAP and/or a GAP-associated protein.

authors

Gschwendt M,Kittstein W,Marks F

doi

10.1006/bbrc.1993.1858

subject

Has Abstract

pub_date

1993-07-15 00:00:00

pages

571-6

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(83)71858-9

journal_volume

194

pub_type

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