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

被引：14

作者：

GSCHWENDT, M

KITTSTEIN, W

MARKS, F

机构：

[1] German Cancer Research Center, D-6900 Heidelberg

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1993年 / 194卷 / 01期

关键词：

D O I：

10.1006/bbrc.1993.1858

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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. © 1993 Academic Press, Inc.

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页码：571 / 576

页数：6

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