| http://purl.uniprot.org/citations/8657103 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/8657103 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/8657103 | http://www.w3.org/2000/01/rdf-schema#comment | "Antigen receptor ligation on lymphocytes activates protein tyrosine kinases and phospholipase C-gamma (PLC-gamma) isoforms. Glutathione S-transferase fusion proteins containing the C-terminal Src-homology 2 [SH2(C)] domain of PLC-gamma1 bound to tyrosyl phosphorylated Syk. Syk isolated from antigen receptor-activated B cells phosphorylated PLC-gamma1 on Tyr-771 and the key regulatory residue Tyr-783 in vitro, whereas Lyn from the same B cells phosphorylated PLC-gamma1 only on Tyr-771. The ability of Syk to phosphorylate PLC-gamma1 required antigen receptor ligation, while Lyn was constitutively active. An mCD8-Syk cDNA construct could be expressed as a tyrosyl-phosphorylated chimeric protein tyrosine kinase in COS cells, was recognized by PLC-gamma1 SH2(C) in vitro, and induced tyrosyl phosphorylation of endogenous PLC-gamma1 in vivo. Substitution of Tyr-525 and Tyr-526 at the autophosphorylation site of Syk in mCD8-Syk substantially reduced the kinase activity and the binding of this variant chimera to PLC-gamma1 SH2(C) in vitro; it also failed to induce tyrosyl phosphorylation of PLC-gamma1 in vivo. In contrast, substitution of Tyr-348 and Tyr-352 in the linker region of Syk in mCD8-Syk did not affect the kinase activity of this variant chimera but almost completely eliminated its binding to PLC-gamma1 SH(C) and completely eliminated its ability to induce tyrosyl phosphorylation of PLC-gamma1 in vivo. Thus, an optimal kinase activity of Syk and an interaction between the linker region of Syk with PLC-gamma1 are required for the tyrosyl phosphorylation of PLC-gamma1."xsd:string |
| http://purl.uniprot.org/citations/8657103 | http://purl.org/dc/terms/identifier | "doi:10.1128/mcb.16.4.1305"xsd:string |
| http://purl.uniprot.org/citations/8657103 | http://purl.org/dc/terms/identifier | "doi:10.1128/mcb.16.4.1305"xsd:string |
| http://purl.uniprot.org/citations/8657103 | http://purl.uniprot.org/core/author | "Clark E.A."xsd:string |
| http://purl.uniprot.org/citations/8657103 | http://purl.uniprot.org/core/author | "Clark E.A."xsd:string |
| http://purl.uniprot.org/citations/8657103 | http://purl.uniprot.org/core/author | "Chandran K.A."xsd:string |
| http://purl.uniprot.org/citations/8657103 | http://purl.uniprot.org/core/author | "Chandran K.A."xsd:string |
| http://purl.uniprot.org/citations/8657103 | http://purl.uniprot.org/core/author | "Law C.L."xsd:string |
| http://purl.uniprot.org/citations/8657103 | http://purl.uniprot.org/core/author | "Law C.L."xsd:string |
| http://purl.uniprot.org/citations/8657103 | http://purl.uniprot.org/core/author | "Sidorenko S.P."xsd:string |
| http://purl.uniprot.org/citations/8657103 | http://purl.uniprot.org/core/author | "Sidorenko S.P."xsd:string |
| http://purl.uniprot.org/citations/8657103 | http://purl.uniprot.org/core/date | "1996"xsd:gYear |
| http://purl.uniprot.org/citations/8657103 | http://purl.uniprot.org/core/date | "1996"xsd:gYear |
| http://purl.uniprot.org/citations/8657103 | http://purl.uniprot.org/core/name | "Mol. Cell. Biol."xsd:string |
| http://purl.uniprot.org/citations/8657103 | http://purl.uniprot.org/core/name | "Mol. Cell. Biol."xsd:string |
| http://purl.uniprot.org/citations/8657103 | http://purl.uniprot.org/core/pages | "1305-1315"xsd:string |
| http://purl.uniprot.org/citations/8657103 | http://purl.uniprot.org/core/pages | "1305-1315"xsd:string |
| http://purl.uniprot.org/citations/8657103 | http://purl.uniprot.org/core/title | "Phospholipase C-gamma1 interacts with conserved phosphotyrosyl residues in the linker region of Syk and is a substrate for Syk."xsd:string |
| http://purl.uniprot.org/citations/8657103 | http://purl.uniprot.org/core/title | "Phospholipase C-gamma1 interacts with conserved phosphotyrosyl residues in the linker region of Syk and is a substrate for Syk."xsd:string |
| http://purl.uniprot.org/citations/8657103 | http://purl.uniprot.org/core/volume | "16"xsd:string |
| http://purl.uniprot.org/citations/8657103 | http://purl.uniprot.org/core/volume | "16"xsd:string |
| http://purl.uniprot.org/citations/8657103 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/8657103 |
| http://purl.uniprot.org/citations/8657103 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/8657103 |