Linked Life Data

10570971

Source:http://linkedlifedata.com/resource/pubmed/id/10570971

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1999-12-2
pubmed:databankReference
pubmed:abstractText
The Rho family of small GTPases and their associated regulators and targets are essential mediators of diverse morphogenetic events in development. Mammalian Rho-kinase/ROK alpha, one of the targets of Rho, has been shown to bind to Rho in GTP-bound form and to phosphorylate the myosin light chain (MLC) and the myosin-binding subunit (MBS) of myosin phosphatase, resulting in the activation of myosin. Thus, Rho-kinase/ROK alpha has been suggested to play essential roles in the formation of stress fibers and focal adhesions. We have identified the Drosophila homolog of Rho-kinase/ROK alpha, DRho-kinase, which has conserved the basic structural feature of Rho-kinase/ROK alpha consisting of the N-terminal kinase, central coiled-coil and C-terminal pleckstrin homology (PH) domains. A two-hybrid analysis demonstrated that DRho-kinase interacts with the GTP-bound form of the Drosophila Rho. Drho1, at the conserved Rho-binding site. DRho-kinase can phosphorylate MLC and MBS, preferable substrates for bovine Rho-kinase, in vitro. DRho-kinase is ubiquitously expressed throughout development, in a pattern essentially identical to that of Drho1. These results suggest that DRho-kinase is an effector of Drho1.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0378-1119
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
238
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
437-44
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
1999
pubmed:articleTitle
Identification and characterization of Drosophila homolog of Rho-kinase.
pubmed:affiliation
Division of Biological Science, Graduate School of Science, Nagoya University, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't