Vasodilator-stimulated phosphoprotein is a substrate for protein kinase C

被引：42

作者：

Chitaley, K ^{[1
]}

Chen, L

Galler, A

Walter, U

Daum, G

Clowes, AW

机构：

[1] Univ Washington, Dept Surg, Seattle, WA 98195 USA

[2] Univ Wurzburg, Inst Klin Biochem & Pathobiochem, Wurzburg, Germany

来源：

FEBS LETTERS | 2004年 / 556卷 / 1-3期

关键词：

phosphorylation; Ser/Thr kinase; focal adhesion;

D O I：

10.1016/S0014-5793(03)01435-2

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：

Vasodilator-stimulated phosphoprotein (VASP), an actin binding protein localized to areas of focal contacts, is a substrate for the cyclic adenosine monophosphate/cyclic guanosine monophosphate (cAMP/cGMP)-dependent protein kinases (PKA, PKG). In this study, we show that serum stimulation of vascular smooth muscle cells (SMCs) induces VASP phosphorylation on Ser157, in a mechanism not dependent on PKA or PKG. We tested the possibility that protein kinase C (PKC), a regulator of cytoskeletal function, is involved. PKC inhibition or down-regulation prevented serum-induced phosphorylation of VASP at Ser157 in rat vascular SMCs. Additionally, recombinant PKCalpha directly phosphorylated Ser157 on VASP. In summary, our data support the hypothesis that PKC phosphorylates VASP and mediates serum-induced VASP regulation. (C) 2003 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

引用

页码：211 / 215

页数：5

共 35 条

[1] The vasodilator-stimulated phosphoprotein (VASP) is involved in cGMP- and cAMP-mediated inhibition of agonist-induced platelet aggregation, but is dispensable for smooth muscle function [J].