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http://purl.uniprot.org/citations/15096500http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15096500http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15096500http://www.w3.org/2000/01/rdf-schema#comment"Activators of G-protein signaling 1-3 (AGS1-3) were identified in a functional screen of mammalian cDNAs that activated G-protein signaling in the absence of a receptor. We report the isolation and characterization of an additional AGS protein (AGS4) from a human prostate leiomyosarcoma cDNA library. AGS4 is identical to G18.1b, which is encoded by a gene within the major histocompatibility class III region of chromosome 6. The activity of AGS4 in the yeast-based functional screen was selective for G(i2)/G(i3) and independent of guanine-nucleotide exchange by G(i)alpha. RNA blots indicated enrichment of AGS4/G18.1b mRNA in heart, placenta, lung, and liver. Immunocytochemistry with AGS4/G18.1b-specific antisera indicated a predominant nonhomogeneous, extranuclear distribution within the cell following expression in COS7 or Chinese hamster ovary cells. AGS4/G18.1b contains three G-protein regulatory motifs downstream of an amino terminus domain with multiple prolines. Glutathione S-transferase (GST)-AGS4/G18.1b fusion proteins interacted with purified G(i)alpha, and peptides derived from each of the G-protein regulatory motifs inhibited guanosine 5'-3-O-(thio)triphosphate (GTPgammaS) binding to purified G(i)alpha(1). AGS4/G18.1b was also complexed with G(i)alpha(3) in COS7 cell lysates following cell transfection. However, AGS4/G18.1b did not alter the generation of inositol phosphates in COS7 cells cotransfected with the Gbetagamma-regulated effector phospholipase C-beta2. These data suggest either that an additional signal is required to position AGS4/G18.1b in the proper cellular location where it can access heterotrimer and promote subunit dissociation or that AGS4 serves as an alternative binding partner for G(i)alpha independent of Gbetagamma participating in G-protein signaling events that are independent of classical G-protein-coupled receptors at the cell surface."xsd:string
http://purl.uniprot.org/citations/15096500http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m312786200"xsd:string
http://purl.uniprot.org/citations/15096500http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m312786200"xsd:string
http://purl.uniprot.org/citations/15096500http://purl.uniprot.org/core/author"Cao X."xsd:string
http://purl.uniprot.org/citations/15096500http://purl.uniprot.org/core/author"Cao X."xsd:string
http://purl.uniprot.org/citations/15096500http://purl.uniprot.org/core/author"Sato M."xsd:string
http://purl.uniprot.org/citations/15096500http://purl.uniprot.org/core/author"Sato M."xsd:string
http://purl.uniprot.org/citations/15096500http://purl.uniprot.org/core/author"Lanier S.M."xsd:string
http://purl.uniprot.org/citations/15096500http://purl.uniprot.org/core/author"Lanier S.M."xsd:string
http://purl.uniprot.org/citations/15096500http://purl.uniprot.org/core/author"Cismowski M.J."xsd:string
http://purl.uniprot.org/citations/15096500http://purl.uniprot.org/core/author"Cismowski M.J."xsd:string
http://purl.uniprot.org/citations/15096500http://purl.uniprot.org/core/author"Blumer J.B."xsd:string
http://purl.uniprot.org/citations/15096500http://purl.uniprot.org/core/author"Blumer J.B."xsd:string
http://purl.uniprot.org/citations/15096500http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15096500http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15096500http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/15096500http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/15096500http://purl.uniprot.org/core/pages"27567-27574"xsd:string
http://purl.uniprot.org/citations/15096500http://purl.uniprot.org/core/pages"27567-27574"xsd:string
http://purl.uniprot.org/citations/15096500http://purl.uniprot.org/core/title"Identification and characterization of AGS4: a protein containing three G-protein regulatory motifs that regulate the activation state of Gialpha."xsd:string
http://purl.uniprot.org/citations/15096500http://purl.uniprot.org/core/title"Identification and characterization of AGS4: a protein containing three G-protein regulatory motifs that regulate the activation state of Gialpha."xsd:string
http://purl.uniprot.org/citations/15096500http://purl.uniprot.org/core/volume"279"xsd:string
http://purl.uniprot.org/citations/15096500http://purl.uniprot.org/core/volume"279"xsd:string
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