Linked Life Data

20374714

Source:http://linkedlifedata.com/resource/pubmed/id/20374714

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2010-4-8
pubmed:abstractText
All regulator of G protein signaling (RGS) proteins contain a conserved domain of approximately 130 amino acids that binds to activated heterotrimeric G protein ? subunits (G?) and accelerates their rate of GTP hydrolysis. Homologous domains are found in at least six other protein families, including a family of Rho guanine nucleotide exchange factors (RhoGEFs) and the G protein-coupled receptor kinases (GRKs). Although some of the RhoGEF and GRK RGS-like domains can also bind to activated G? subunits, they do so in distinct ways and with much lower levels of GTPase activation. In other protein families, the domains have as of yet no obvious relationship to heterotrimeric G protein signaling. These RGS homology (RH) domains are now recognized as mediators of extraordinarily diverse protein-protein interactions. Through these interactions, they play roles that range from enzyme to molecular scaffold to signal transducing module. In this review, the atomic structures of RH domains from RGS proteins, Axins, RhoGEFs, and GRKs are compared in light of what is currently known about their functional roles.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1878-0814
pubmed:author
pubmed:copyrightInfo
Copyright © 2009 Elsevier Inc. All rights reserved.
pubmed:issnType
Electronic
pubmed:volume
86
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
75-113
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
Structure and function of regulator of G protein signaling homology domains.
pubmed:affiliation
Department of Pharmacology, Life Sciences Institute, University of Michigan, Ann Arbor, Michigan 48109?2216, USA.
pubmed:publicationType
Journal Article, Review, Research Support, N.I.H., Extramural