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http://purl.uniprot.org/citations/21725281http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/21725281http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/21725281http://www.w3.org/2000/01/rdf-schema#comment"Cooperatively assembled signalling complexes, nucleated by adaptor proteins, integrate information from surface receptors to determine cellular outcomes. In T and mast cells, antigen receptor signalling is nucleated by three adaptors: SLP-76, Gads and LAT. Three well-characterized SLP-76 tyrosine phosphorylation sites recruit key components, including a Tec-family tyrosine kinase, Itk. We identified a fourth, evolutionarily conserved SLP-76 phosphorylation site, Y173, which was phosphorylated upon T-cell receptor stimulation in primary murine and Jurkat T cells. Y173 was required for antigen receptor-induced phosphorylation of phospholipase C-γ1 (PLC-γ1) in both T and mast cells, and for consequent downstream events, including activation of the IL-2 promoter in T cells, and degranulation and IL-6 production in mast cells. In intact cells, Y173 phosphorylation depended on three, ZAP-70-targeted tyrosines at the N-terminus of SLP-76 that recruit and activate Itk, a kinase that selectively phosphorylated Y173 in vitro. These data suggest a sequential mechanism whereby ZAP-70-dependent priming of SLP-76 at three N-terminal sites triggers reciprocal regulatory interactions between Itk and SLP-76, which are ultimately required to couple active Itk to its substrate, PLC-γ1."xsd:string
http://purl.uniprot.org/citations/21725281http://purl.org/dc/terms/identifier"doi:10.1038/emboj.2011.213"xsd:string
http://purl.uniprot.org/citations/21725281http://purl.org/dc/terms/identifier"doi:10.1038/emboj.2011.213"xsd:string
http://purl.uniprot.org/citations/21725281http://purl.uniprot.org/core/author"Beach D."xsd:string
http://purl.uniprot.org/citations/21725281http://purl.uniprot.org/core/author"Beach D."xsd:string
http://purl.uniprot.org/citations/21725281http://purl.uniprot.org/core/author"Urlaub H."xsd:string
http://purl.uniprot.org/citations/21725281http://purl.uniprot.org/core/author"Urlaub H."xsd:string
http://purl.uniprot.org/citations/21725281http://purl.uniprot.org/core/author"Okumura M."xsd:string
http://purl.uniprot.org/citations/21725281http://purl.uniprot.org/core/author"Okumura M."xsd:string
http://purl.uniprot.org/citations/21725281http://purl.uniprot.org/core/author"Chernoff J."xsd:string
http://purl.uniprot.org/citations/21725281http://purl.uniprot.org/core/author"Chernoff J."xsd:string
http://purl.uniprot.org/citations/21725281http://purl.uniprot.org/core/author"Wienands J."xsd:string
http://purl.uniprot.org/citations/21725281http://purl.uniprot.org/core/author"Wienands J."xsd:string
http://purl.uniprot.org/citations/21725281http://purl.uniprot.org/core/author"Kambayashi T."xsd:string
http://purl.uniprot.org/citations/21725281http://purl.uniprot.org/core/author"Kambayashi T."xsd:string
http://purl.uniprot.org/citations/21725281http://purl.uniprot.org/core/author"Oellerich T."xsd:string
http://purl.uniprot.org/citations/21725281http://purl.uniprot.org/core/author"Oellerich T."xsd:string
http://purl.uniprot.org/citations/21725281http://purl.uniprot.org/core/author"Yablonski D."xsd:string
http://purl.uniprot.org/citations/21725281http://purl.uniprot.org/core/author"Yablonski D."xsd:string
http://purl.uniprot.org/citations/21725281http://purl.uniprot.org/core/author"Koretzky G."xsd:string
http://purl.uniprot.org/citations/21725281http://purl.uniprot.org/core/author"Koretzky G."xsd:string
http://purl.uniprot.org/citations/21725281http://purl.uniprot.org/core/author"Bogin Y."xsd:string
http://purl.uniprot.org/citations/21725281http://purl.uniprot.org/core/author"Bogin Y."xsd:string