Linked Life Data

16472651

Source:http://linkedlifedata.com/resource/pubmed/id/16472651

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2006-2-13
pubmed:abstractText
Rho GTPase activation is partially regulated at the level of guanine nucleotide dissociation inhibitors, or GDIs. The binding of Rho GTPases to GDIs has been shown to dramatically reduce the action of guanine nucleotide exchange factors (GEFs) to initiate Rho GTPase activation. The GDI-GTPase complex thus serves as a major point of regulation of Rho GTPase activity and function. It is likely that specific mechanisms exist to dissociate individual members of the Rho GTPase family from cytosolic Rho GDI complexes to facilitate the activation process. Such dissociation would likely be tightly coupled to GEF-mediated guanine nucleotide exchange and membrane association of the activated GTPase, resulting in effector binding and functional responses. Accumulating evidence suggests that the phosphorylation of either the Rho GTPases themselves and/or phosphorylation of GDIs might serve as a mechanism for regulating the formation and/or dissociation of Rho GTPase-GDI complexes. Indeed, the selective release of Rac1 from RhoGDI complexes induced by the p21-activated kinase-regulated phosphorylation of RhoGDI has been reported. We describe here methods for the analysis of RhoGDI phosphorylation and regulation by p21-activated kinase 1 (Pak1).
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0076-6879
pubmed:author
pubmed:issnType
Print
pubmed:volume
406
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
80-90
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
2006
pubmed:articleTitle
Phosphorylation of RhoGDI by p21-activated kinase 1.
pubmed:affiliation
Department of Immunology and Cell Biology, The Scripps Research Institute, La Jolla, CA, USA.
pubmed:publicationType
Journal Article