Linked Life Data

10903897

Source:http://linkedlifedata.com/resource/pubmed/id/10903897

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2000-8-31
pubmed:abstractText
mDial is a downstream target molecule of Rho small G protein and regulates the formation of parallel stress fibers in MDCK cells. mDial consists of at least one Rho-binding domain (RBD), one FH3 domain (FH3D), one coiled-coil domain (CCD), one FH1 domain (FH1D), one FH2 domain (FH2D), and another CCD in this order from the N-terminus to the C-terminus. We constructed various deletion mutants of mDial and investigated the mechanisms of its activation and action by measuring the formation of parallel stress fibers in MDCK cells. We show here that at least FH1D and second CCD are essential for the formation of parallel stress fibers. Furthermore, we present the evidence suggesting that mDial has another domain which interacts with RBD, that this interaction masks FH1D and second CCD and keeps mDial inactive, and that the binding of Rho to RBD opens this folded structure, resulting in the activation of mDial.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0006-291X
pubmed:author
pubmed:copyrightInfo
Copyright 2000 Academic Press.
pubmed:issnType
Print
pubmed:day
21
pubmed:volume
274
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
68-72
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2000
pubmed:articleTitle
Mechanisms of activation and action of mDial in the formation of parallel stress fibers in MDCK cells.
pubmed:affiliation
Department of Molecular Biology and Biochemistry, Osaka University Graduate School of Medicine/Faculty of Medicine, Suita, 565-0871, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't