RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/11387333http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11387333http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11387333http://www.w3.org/2000/01/rdf-schema#comment"The regulators of G-protein signaling (RGS) proteins accelerate the intrinsic guanosine triphosphatase activity of heterotrimeric G-protein alpha subunits and are thus recognized as key modulators of G-protein-coupled receptor signaling. RGS12 and RGS14 contain not only the hallmark RGS box responsible for GTPase-accelerating activity but also a single G alpha(i/o)-Loco (GoLoco) motif predicted to represent a second G alpha interaction site. Here, we describe functional characterization of the GoLoco motif regions of RGS12 and RGS14. Both regions interact exclusively with G alpha(i1), G alpha(i2), and G alpha(i3) in their GDP-bound forms. In GTP gamma S binding assays, both regions exhibit guanine nucleotide dissociation inhibitor (GDI) activity, inhibiting the rate of exchange of GDP for GTP by G alpha(i1). Both regions also stabilize G alpha(i1) in its GDP-bound form, inhibiting the increase in intrinsic tryptophan fluorescence stimulated by AlF(4)(-). Our results indicate that both RGS12 and RGS14 harbor two distinctly different G alpha interaction sites: a previously recognized N-terminal RGS box possessing G alpha(i/o) GAP activity and a C-terminal GoLoco region exhibiting G alpha(i) GDI activity. The presence of two, independent G alpha interaction sites suggests that RGS12 and RGS14 participate in a complex coordination of G-protein signaling beyond simple G alpha GAP activity."xsd:string
http://purl.uniprot.org/citations/11387333http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m103208200"xsd:string
http://purl.uniprot.org/citations/11387333http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m103208200"xsd:string
http://purl.uniprot.org/citations/11387333http://purl.uniprot.org/core/author"Siderovski D.P."xsd:string
http://purl.uniprot.org/citations/11387333http://purl.uniprot.org/core/author"Siderovski D.P."xsd:string
http://purl.uniprot.org/citations/11387333http://purl.uniprot.org/core/author"Morris R.A."xsd:string
http://purl.uniprot.org/citations/11387333http://purl.uniprot.org/core/author"Morris R.A."xsd:string
http://purl.uniprot.org/citations/11387333http://purl.uniprot.org/core/author"Tronchere H."xsd:string
http://purl.uniprot.org/citations/11387333http://purl.uniprot.org/core/author"Tronchere H."xsd:string
http://purl.uniprot.org/citations/11387333http://purl.uniprot.org/core/author"De Vries L."xsd:string
http://purl.uniprot.org/citations/11387333http://purl.uniprot.org/core/author"De Vries L."xsd:string
http://purl.uniprot.org/citations/11387333http://purl.uniprot.org/core/author"Behe C.I."xsd:string
http://purl.uniprot.org/citations/11387333http://purl.uniprot.org/core/author"Behe C.I."xsd:string
http://purl.uniprot.org/citations/11387333http://purl.uniprot.org/core/author"Gist Farquhar M."xsd:string
http://purl.uniprot.org/citations/11387333http://purl.uniprot.org/core/author"Gist Farquhar M."xsd:string
http://purl.uniprot.org/citations/11387333http://purl.uniprot.org/core/author"Kimple R.J."xsd:string
http://purl.uniprot.org/citations/11387333http://purl.uniprot.org/core/author"Kimple R.J."xsd:string
http://purl.uniprot.org/citations/11387333http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11387333http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11387333http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/11387333http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/11387333http://purl.uniprot.org/core/pages"29275-29281"xsd:string
http://purl.uniprot.org/citations/11387333http://purl.uniprot.org/core/pages"29275-29281"xsd:string