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http://purl.uniprot.org/citations/20154219http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20154219http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20154219http://www.w3.org/2000/01/rdf-schema#comment"The C-type lectin receptor CLEC-2 activates platelets through Src and Syk tyrosine kinases, leading to tyrosine phosphorylation of downstream adapter proteins and effector enzymes, including phospholipase-C gamma2. Signaling is initiated through phosphorylation of a single conserved tyrosine located in a YxxL sequence in the CLEC-2 cytosolic tail. The signaling pathway used by CLEC-2 shares many similarities with that used by receptors that have 1 or more copies of an immunoreceptor tyrosine-based activation motif, defined by the sequence Yxx(L/I)x(6-12)Yxx(L/I), in their cytosolic tails or associated receptor chains. Phosphorylation of the conserved immunoreceptor tyrosine-based activation motif tyrosines promotes Syk binding and activation through binding of the Syk tandem SH2 domains. In this report, we present evidence using peptide pull-down studies, surface plasmon resonance, quantitative Western blotting, tryptophan fluorescence measurements, and competition experiments that Syk activation by CLEC-2 is mediated by the cross-linking through the tandem SH2 domains with a stoichiometry of 2:1. In support of this model, cross-linking and electron microscopy demonstrate that CLEC-2 is present as a dimer in resting platelets and converted to larger complexes on activation. This is a unique mode of activation of Syk by a single YxxL-containing receptor."xsd:string
http://purl.uniprot.org/citations/20154219http://purl.org/dc/terms/identifier"doi:10.1182/blood-2009-08-237834"xsd:string
http://purl.uniprot.org/citations/20154219http://purl.org/dc/terms/identifier"doi:10.1182/blood-2009-08-237834"xsd:string
http://purl.uniprot.org/citations/20154219http://purl.uniprot.org/core/author"Pollitt A.Y."xsd:string
http://purl.uniprot.org/citations/20154219http://purl.uniprot.org/core/author"Pollitt A.Y."xsd:string
http://purl.uniprot.org/citations/20154219http://purl.uniprot.org/core/author"Mori J."xsd:string
http://purl.uniprot.org/citations/20154219http://purl.uniprot.org/core/author"Mori J."xsd:string
http://purl.uniprot.org/citations/20154219http://purl.uniprot.org/core/author"Eble J.A."xsd:string
http://purl.uniprot.org/citations/20154219http://purl.uniprot.org/core/author"Eble J.A."xsd:string
http://purl.uniprot.org/citations/20154219http://purl.uniprot.org/core/author"Hartwig J.H."xsd:string
http://purl.uniprot.org/citations/20154219http://purl.uniprot.org/core/author"Hartwig J.H."xsd:string
http://purl.uniprot.org/citations/20154219http://purl.uniprot.org/core/author"Hughes C.E."xsd:string
http://purl.uniprot.org/citations/20154219http://purl.uniprot.org/core/author"Hughes C.E."xsd:string
http://purl.uniprot.org/citations/20154219http://purl.uniprot.org/core/author"Tomlinson M.G."xsd:string
http://purl.uniprot.org/citations/20154219http://purl.uniprot.org/core/author"Tomlinson M.G."xsd:string
http://purl.uniprot.org/citations/20154219http://purl.uniprot.org/core/author"Watson S.P."xsd:string
http://purl.uniprot.org/citations/20154219http://purl.uniprot.org/core/author"Watson S.P."xsd:string
http://purl.uniprot.org/citations/20154219http://purl.uniprot.org/core/author"Fuetterer K."xsd:string
http://purl.uniprot.org/citations/20154219http://purl.uniprot.org/core/author"Fuetterer K."xsd:string
http://purl.uniprot.org/citations/20154219http://purl.uniprot.org/core/author"O'Callaghan C.A."xsd:string
http://purl.uniprot.org/citations/20154219http://purl.uniprot.org/core/author"O'Callaghan C.A."xsd:string
http://purl.uniprot.org/citations/20154219http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/20154219http://purl.uniprot.org/core/date"2010"xsd:gYear