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PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2004-10-18
pubmed:abstractText
G-protein-coupled receptor kinases (GRKs) specifically phosphorylate agonist-occupied G-protein-coupled receptors (GPCRs). All seven mammalian GRKs contain an N-terminal domain that is homologous to the regulator of G-protein signaling (RGS) family of proteins. The RGS domain of GRK2 has been shown to interact specifically with Galphaq family members. While the specificity and functional consequences of GRK/Galpha interaction remain somewhat poorly defined, GRK RGS homology (RH) domains likely function to provide specificity for GRK interaction with a particular Galpha subunit or GPCR/Galpha complex. Indeed, GRK2 binds Galphaq, alpha11, and alpha14, but not Galpha16, Galphas, Galphai, or Galpha(12/13), while the RGS domains of GRK5 and GRK6 do not bind Galpha(q/11), Galphas, Galphai, or Galpha(12/13). In this chapter we describe various in vitro and intact cell strategies that can be used to elucidate the function of GRK RH domains.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0076-6879
pubmed:author
pubmed:issnType
Print
pubmed:volume
390
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
295-310
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
2004
pubmed:articleTitle
Analysis of G-protein-coupled receptor kinase RGS homology domains.
pubmed:affiliation
Department of Microbiology and Immunology, Thomas Jefferson University, Philadelphia, Pennsylvania 19107, USA.
pubmed:publicationType
Journal Article