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Does Vav bind to F‐actin through a CH domain?
Author(s) -
Castresana Jose,
Saraste Matti
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)01098-y
Subject(s) - calponin , actin , microbiology and biotechnology , actin cytoskeleton , cytoskeleton , actin binding protein , chemistry , domain (mathematical analysis) , actina , binding domain , homology (biology) , biology , biochemistry , binding site , amino acid , cell , mathematical analysis , mathematics
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 α‐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.