| http://purl.uniprot.org/citations/15161916 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/15161916 | http://www.w3.org/2000/01/rdf-schema#comment | "Phospholipase C-gamma 1 (PLC-gamma 1) is phosphorylated on three tyrosine residues: Tyr-771, Tyr-783, and Tyr-1253. With the use of antibodies specific for each of these phosphorylation sites, we have now determined the kinetics and magnitude of phosphorylation at each site. Phosphorylation of Tyr-783, which is essential for lipase activation, was observed in all stimulated cell types examined. The extent of phosphorylation of Tyr-1253 was approximately 50 to 70% of that of Tyr-783 in cells stimulated with platelet-derived growth factor (PDGF) or epidermal growth factor (EGF), but Tyr-1253 phosphorylation was not detected in B or T cell lines stimulated through B- and T-cell antigen receptors, respectively. Tyr-771 was phosphorylated only at a low level in all cells studied. In cells stimulated with PDGF, phosphorylation and dephosphorylation of Tyr-783 and of Tyr-1253 occurred with similar kinetics; the receptor kinase appeared to phosphorylate both sites, albeit with Tyr-783 favored over Tyr-1253, before the bound PLC-gamma 1 was released, and phosphorylation at the two sites occurred independently. PDGF and EGF induced similar levels of phosphorylation of Tyr-783 and of Tyr-1253 in a cell line that expressed receptors for both growth factors. However, only PDGF, not EGF, elicited substantial PLC activity, suggesting that Tyr-783 phosphorylation was not sufficient for enzyme activation. Finally, concurrent production of phosphatidylinositol 3,4,5-trisphosphate was found to contribute to the activation of phosphorylated PLC-gamma 1."xsd:string |
| http://purl.uniprot.org/citations/15161916 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m405116200"xsd:string |
| http://purl.uniprot.org/citations/15161916 | http://purl.uniprot.org/core/author | "Kim Y.J."xsd:string |
| http://purl.uniprot.org/citations/15161916 | http://purl.uniprot.org/core/author | "Rhee S.G."xsd:string |
| http://purl.uniprot.org/citations/15161916 | http://purl.uniprot.org/core/author | "Poulin B."xsd:string |
| http://purl.uniprot.org/citations/15161916 | http://purl.uniprot.org/core/author | "Sekiya F."xsd:string |
| http://purl.uniprot.org/citations/15161916 | http://purl.uniprot.org/core/date | "2004"xsd:gYear |
| http://purl.uniprot.org/citations/15161916 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/15161916 | http://purl.uniprot.org/core/pages | "32181-32190"xsd:string |
| http://purl.uniprot.org/citations/15161916 | http://purl.uniprot.org/core/title | "Mechanism of tyrosine phosphorylation and activation of phospholipase C-gamma 1. Tyrosine 783 phosphorylation is not sufficient for lipase activation."xsd:string |
| http://purl.uniprot.org/citations/15161916 | http://purl.uniprot.org/core/volume | "279"xsd:string |
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