Linked Life Data

15707985

Source:http://linkedlifedata.com/resource/pubmed/id/15707985

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2005-2-14
pubmed:abstractText
In yeast, Verprolin plays an important role in rearrangement of the actin cytoskeleton. There are three mammalian homologues of Verprolin, WIP, CR16, and WICH, and all of them bind actin and Wiskott-Aldrich syndrome protein (WASP) and/or neural-WASP. Here, we describe a novel function of WICH. In vitro co-sedimentation analysis revealed that WICH not only binds to actin filaments but also cross-links them. Fluorescence and electron microscopy detected that this cross-linking results in straight bundled actin filaments. Overexpression of WICH alone in cultured fibroblast caused the formation of thick actin fibers. This ability of WICH depended on its own actin cross-linking activity. Importantly, the actin cross-linking activity of WICH was modified through a direct association with N-WASP. Taken together, these data suggest that WICH induces a bundled form of actin filament with actin cross-linking activity and the association with N-WASP suppresses that activity. WICH thus appears to be a novel actin bundling protein.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
328
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1058-66
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed:year
2005
pubmed:articleTitle
WICH, a member of WASP-interacting protein family, cross-links actin filaments.
pubmed:affiliation
Department of Biochemistry, Institute of Medical Science, University of Tokyo, 4-6-1 Shirokanedai, Mianato-ku, Tokyo 108-8639, Japan.
pubmed:publicationType
Journal Article