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http://purl.uniprot.org/citations/17681949http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17681949http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17681949http://www.w3.org/2000/01/rdf-schema#comment"The family of SLPs (Src homology 2 domain-containing leukocyte adaptor proteins) are cytoplasmic signal effectors of lymphocyte antigen receptors. A main function of SLP is to orchestrate the assembly of Ca(2+)-mobilizing enzymes at the inner leaflet of the plasma membrane. For this purpose, SLP-76 in T cells utilizes the transmembrane adaptor LAT, but the mechanism of SLP-65 membrane anchoring in B cells remains an enigma. We now employed two genetic reconstitution systems to unravel structural requirements of SLP-65 for the initiation of Ca(2+) mobilization and subsequent activation of gene transcription. First, mutational analysis of SLP-65 in DT40 B cells revealed that its C-terminal Src homology 2 domain controls efficient tyrosine phosphorylation by the kinase Syk, plasma membrane recruitment, as well as downstream signaling to NFAT activation. Second, we dissected these processes by expressing SLP-65 in SLP-76-deficient T cells and found that a kinase-independent adaptor function of Syk is required to link phosphorylated SLP-65 to Ca(2+) mobilization. These approaches unmask a mechanistic complexity of SLP-65 activation and coupling to signaling cascades in that Syk is upstream as well as downstream of SLP-65. Moreover, membrane anchoring of the SLP-65-assembled Ca(2+) initiation complex, which appears to be fundamentally different from that of closely related SLP-76, does not necessarily involve a B cell-specific component."xsd:string
http://purl.uniprot.org/citations/17681949http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m704043200"xsd:string
http://purl.uniprot.org/citations/17681949http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m704043200"xsd:string
http://purl.uniprot.org/citations/17681949http://purl.uniprot.org/core/author"Abudula A."xsd:string
http://purl.uniprot.org/citations/17681949http://purl.uniprot.org/core/author"Abudula A."xsd:string
http://purl.uniprot.org/citations/17681949http://purl.uniprot.org/core/author"Brechmann M."xsd:string
http://purl.uniprot.org/citations/17681949http://purl.uniprot.org/core/author"Brechmann M."xsd:string
http://purl.uniprot.org/citations/17681949http://purl.uniprot.org/core/author"Dittmann K."xsd:string
http://purl.uniprot.org/citations/17681949http://purl.uniprot.org/core/author"Dittmann K."xsd:string
http://purl.uniprot.org/citations/17681949http://purl.uniprot.org/core/author"Goldbeck I."xsd:string
http://purl.uniprot.org/citations/17681949http://purl.uniprot.org/core/author"Goldbeck I."xsd:string
http://purl.uniprot.org/citations/17681949http://purl.uniprot.org/core/author"Grabbe A."xsd:string
http://purl.uniprot.org/citations/17681949http://purl.uniprot.org/core/author"Grabbe A."xsd:string
http://purl.uniprot.org/citations/17681949http://purl.uniprot.org/core/author"Herrmann N."xsd:string
http://purl.uniprot.org/citations/17681949http://purl.uniprot.org/core/author"Herrmann N."xsd:string
http://purl.uniprot.org/citations/17681949http://purl.uniprot.org/core/author"Polaschegg C."xsd:string
http://purl.uniprot.org/citations/17681949http://purl.uniprot.org/core/author"Polaschegg C."xsd:string
http://purl.uniprot.org/citations/17681949http://purl.uniprot.org/core/author"Wienands J."xsd:string
http://purl.uniprot.org/citations/17681949http://purl.uniprot.org/core/author"Wienands J."xsd:string
http://purl.uniprot.org/citations/17681949http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17681949http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17681949http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/17681949http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string