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PMID: 7589522 Published · ppublish English Journal Article

Does Vav bind to F-actin through a CH domain?

FEBS letters ·Vol. 374 ·No. 2 ·1995-10-30 ·Pages 149-51

Castresana J, Saraste M

Abstract

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.

MeSH Terms
Actins/metabolism Amino Acid Sequence Animals Carrier Proteins/chemistry,metabolism Cell Cycle Proteins Humans Microfilament Proteins/chemistry,metabolism Molecular Sequence Data Protein Binding Proto-Oncogene Proteins/chemistry,metabolism Proto-Oncogene Proteins c-vav Sequence Homology, Amino Acid
Chemicals
Actins Carrier Proteins Cell Cycle Proteins F-actin-binding proteins Microfilament Proteins Proto-Oncogene Proteins Proto-Oncogene Proteins c-vav VAV1 protein, human
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Castresana J
European Molecular Biology Laboratory, Heidelberg, Germany.
Saraste M
Article Info
Journal
FEBS letters
Abbr.
FEBS Lett
ISSN
0014-5793
Published
1995-10-30
Pages
149-51
Language
English
Region
England
NLM ID
0155157
Subset
IM
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