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http://purl.uniprot.org/citations/16867977http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16867977http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16867977http://www.w3.org/2000/01/rdf-schema#comment"The RGS7 (R7) family of G protein regulators, Gbeta5, and R7BP form heterotrimeric complexes that potently regulate the kinetics of G protein-coupled receptor signaling. Reversible palmitoylation of R7BP regulates plasma membrane/nuclear shuttling of R7*Gbeta5*R7BP heterotrimers. Here we have investigated mechanisms whereby R7BP controls the function of the R7 family. We show that unpalmitoylated R7BP undergoes nuclear/cytoplasmic shuttling and that a C-terminal polybasic motif proximal to the palmitoylation acceptor sites of R7BP mediates nuclear localization, palmitoylation, and plasma membrane targeting. These results suggest a novel mechanism whereby palmitoyltransferases and nuclear import receptors both utilize the C-terminal domain of R7BP to determine the trafficking fate of R7*Gbeta5*R7BP heterotrimers. Analogous mechanisms may regulate other signaling proteins whose distribution between the plasma membrane and nucleus is controlled by palmitoylation. Lastly, we show that cytoplasmic RGS7*Gbeta5*R7BP heterotrimers and RGS7*Gbeta5 heterodimers are equivalently inefficient regulators of G protein-coupled receptor signaling relative to plasma membrane-bound heterotrimers bearing palmitoylated R7BP. Therefore, R7BP augments the function of the complex by a palmitoylation-regulated plasma membrane-targeting mechanism."xsd:string
http://purl.uniprot.org/citations/16867977http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m604428200"xsd:string
http://purl.uniprot.org/citations/16867977http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m604428200"xsd:string
http://purl.uniprot.org/citations/16867977http://purl.uniprot.org/core/author"Linder M.E."xsd:string
http://purl.uniprot.org/citations/16867977http://purl.uniprot.org/core/author"Linder M.E."xsd:string
http://purl.uniprot.org/citations/16867977http://purl.uniprot.org/core/author"Blumer K.J."xsd:string
http://purl.uniprot.org/citations/16867977http://purl.uniprot.org/core/author"Blumer K.J."xsd:string
http://purl.uniprot.org/citations/16867977http://purl.uniprot.org/core/author"Kaltenbronn K.M."xsd:string
http://purl.uniprot.org/citations/16867977http://purl.uniprot.org/core/author"Kaltenbronn K.M."xsd:string
http://purl.uniprot.org/citations/16867977http://purl.uniprot.org/core/author"Huettner J.E."xsd:string
http://purl.uniprot.org/citations/16867977http://purl.uniprot.org/core/author"Huettner J.E."xsd:string
http://purl.uniprot.org/citations/16867977http://purl.uniprot.org/core/author"Drenan R.M."xsd:string
http://purl.uniprot.org/citations/16867977http://purl.uniprot.org/core/author"Drenan R.M."xsd:string
http://purl.uniprot.org/citations/16867977http://purl.uniprot.org/core/author"Buchwalter A.L."xsd:string
http://purl.uniprot.org/citations/16867977http://purl.uniprot.org/core/author"Buchwalter A.L."xsd:string
http://purl.uniprot.org/citations/16867977http://purl.uniprot.org/core/author"Doupnik C.A."xsd:string
http://purl.uniprot.org/citations/16867977http://purl.uniprot.org/core/author"Doupnik C.A."xsd:string
http://purl.uniprot.org/citations/16867977http://purl.uniprot.org/core/author"Jayaraman M."xsd:string
http://purl.uniprot.org/citations/16867977http://purl.uniprot.org/core/author"Jayaraman M."xsd:string
http://purl.uniprot.org/citations/16867977http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/16867977http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/16867977http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/16867977http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string