DOES VAV BIND TO F-ACTIN THROUGH A CH DOMAIN

被引：126

作者：

CASTRESANA, J ^{[1
]}

SARASTE, M ^{[1
]}

机构：

[1] EUROPEAN MOLEC BIOL LAB,D-69012 HEIDELBERG,GERMANY

来源：

FEBS LETTERS | 1995年 / 374卷 / 02期

关键词：

CALPONIN-HOMOLOGY; CYTOSKELETON; SIGNAL TRANSDUCTION; VAV; ACTIN BINDING;

D O I：

10.1016/0014-5793(95)01098-Y

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：

An actin-binding protein domain we call here 'calponin-homology' or CH is present in signalling proteins such as Vav which are involved in activation and inactivation of small G-proteins, Using profile methods, we have detected two repeats of this domain in the actin-binding region of alpha-actinin and related proteins. Based on this, we propose that CH domain in Vav and other signalling proteins is employed for association with filamentous actin, and that this function correlates with their control on the G-proteins Rac and Rho which are involved in the organization of cytoskeleton,

引用

页码：149 / 151

页数：3

共 21 条

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