http://purl.uniprot.org/citations/15184383 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/15184383 | http://www.w3.org/2000/01/rdf-schema#comment | "Tyrosine phosphorylation of phospholipase Cgamma2 (PLCgamma2) is a crucial activation switch that initiates and maintains intracellular calcium mobilization in response to B cell antigen receptor (BCR) engagement. Although members from three distinct families of non-receptor tyrosine kinases can phosphorylate PLCgamma in vitro, the specific kinase(s) controlling BCR-dependent PLCgamma activation in vivo remains unknown. Bruton's tyrosine kinase (Btk)-deficient human B cells exhibit diminished inositol 1,4,5-trisphosphate production and calcium signaling despite a normal inducible level of total PLCgamma2 tyrosine phosphorylation. This suggested that Btk might modify a critical subset of residues essential for PLCgamma2 activity. To evaluate this hypothesis, we generated site-specific phosphotyrosine antibodies recognizing four putative regulatory residues within PLCgamma2. Whereas all four sites were rapidly modified in response to BCR engagement in normal B cells, Btk-deficient B cells exhibited a marked reduction in phosphorylation of the Src homology 2 (SH2)-SH3 linker region sites, Tyr(753) and Tyr(759). Phosphorylation of both sites was restored by expression of Tec, but not Syk, family kinases. In contrast, phosphorylation of the PLCgamma2 carboxyl-terminal sites, Tyr(1197) and Tyr(1217), was unaffected by the absence of functional Btk. Together, these data support a model whereby Btk/Tec kinases control sustained calcium signaling via site-specific phosphorylation of key residues within the PLCgamma2 SH2-SH3 linker."xsd:string |
http://purl.uniprot.org/citations/15184383 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m311985200"xsd:string |
http://purl.uniprot.org/citations/15184383 | http://purl.uniprot.org/core/author | "Kato R.M."xsd:string |
http://purl.uniprot.org/citations/15184383 | http://purl.uniprot.org/core/author | "Rawlings D.J."xsd:string |
http://purl.uniprot.org/citations/15184383 | http://purl.uniprot.org/core/author | "Sommer K."xsd:string |
http://purl.uniprot.org/citations/15184383 | http://purl.uniprot.org/core/author | "Turk C.W."xsd:string |
http://purl.uniprot.org/citations/15184383 | http://purl.uniprot.org/core/author | "Daniel J.L."xsd:string |
http://purl.uniprot.org/citations/15184383 | http://purl.uniprot.org/core/author | "Humphries L.A."xsd:string |
http://purl.uniprot.org/citations/15184383 | http://purl.uniprot.org/core/author | "Dangelmaier C."xsd:string |
http://purl.uniprot.org/citations/15184383 | http://purl.uniprot.org/core/author | "Griffith N."xsd:string |
http://purl.uniprot.org/citations/15184383 | http://purl.uniprot.org/core/author | "Bakman I."xsd:string |
http://purl.uniprot.org/citations/15184383 | http://purl.uniprot.org/core/author | "Kipp K."xsd:string |
http://purl.uniprot.org/citations/15184383 | http://purl.uniprot.org/core/date | "2004"xsd:gYear |
http://purl.uniprot.org/citations/15184383 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
http://purl.uniprot.org/citations/15184383 | http://purl.uniprot.org/core/pages | "37651-37661"xsd:string |
http://purl.uniprot.org/citations/15184383 | http://purl.uniprot.org/core/title | "Tec kinases mediate sustained calcium influx via site-specific tyrosine phosphorylation of the phospholipase Cgamma Src homology 2-Src homology 3 linker."xsd:string |
http://purl.uniprot.org/citations/15184383 | http://purl.uniprot.org/core/volume | "279"xsd:string |
http://purl.uniprot.org/citations/15184383 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/15184383 |
http://purl.uniprot.org/citations/15184383 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/15184383 |
http://purl.uniprot.org/uniprot/#_A0A0C4DH25-mappedCitation-15184383 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/15184383 |
http://purl.uniprot.org/uniprot/#_A0A0C4DH73-mappedCitation-15184383 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/15184383 |
http://purl.uniprot.org/uniprot/#_A0A075B6P5-mappedCitation-15184383 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/15184383 |
http://purl.uniprot.org/uniprot/#_A0A075B6S6-mappedCitation-15184383 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/15184383 |
http://purl.uniprot.org/uniprot/#_P0CF74-mappedCitation-15184383 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/15184383 |