蛋白磷酸酶1和蛋白磷酸酶2A对重组蛋白激酶Cα活性的调节

Regulation of recombinant PKC alpha activity by protein phosphatase 1 and protein phosphatase 2A.

作者信息

Ricciarelli R, Azzi A

机构信息

Institut für Biochemie und Molekularbiologie, Universität Bern, Bühlstrasse 28, Bern, 3012, Switzerland.

出版信息

Arch Biochem Biophys. 1998 Jul 15;355(2):197-200. doi: 10.1006/abbi.1998.0732.

DOI:10.1006/abbi.1998.0732

PMID:9675027

Abstract

The sensitivity of PKC alpha to two protein phosphatases (PP1 and PP2A) has been studied. The results show that both phosphatases reversibly inhibit PKC alpha activity suggesting an effect at PKC autophosphorylation sites and not at transphosphorylation sites. Moreover, PP1 has been found at low concentration to activate PKC alpha implying the existence of an inhibitory phosphorylation site. Further, PKC alpha has been shown to phosphorylate PP2A at its regulatory subunit B.

摘要

已对蛋白激酶Cα（PKCα）对两种蛋白磷酸酶（PP1和PP2A）的敏感性进行了研究。结果表明，这两种磷酸酶均可逆转抑制PKCα活性，提示其作用于PKC的自身磷酸化位点而非转磷酸化位点。此外，已发现低浓度的PP1可激活PKCα，这意味着存在一个抑制性磷酸化位点。此外，PKCα已被证明可在其调节亚基B处使PP2A磷酸化。