| pubmed-article:8657103 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8657103 | lifeskim:mentions | umls-concept:C0205147 | lld:lifeskim |
| pubmed-article:8657103 | lifeskim:mentions | umls-concept:C0031671 | lld:lifeskim |
| pubmed-article:8657103 | lifeskim:mentions | umls-concept:C1709915 | lld:lifeskim |
| pubmed-article:8657103 | lifeskim:mentions | umls-concept:C1710236 | lld:lifeskim |
| pubmed-article:8657103 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:8657103 | pubmed:dateCreated | 1996-7-29 | lld:pubmed |
| pubmed-article:8657103 | pubmed:abstractText | 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. | lld:pubmed |
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| pubmed-article:8657103 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8657103 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8657103 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8657103 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:8657103 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8657103 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:8657103 | pubmed:issn | 0270-7306 | lld:pubmed |
| pubmed-article:8657103 | pubmed:author | pubmed-author:SidorenkoS... | lld:pubmed |
| pubmed-article:8657103 | pubmed:author | pubmed-author:ClarkE AEA | lld:pubmed |
| pubmed-article:8657103 | pubmed:author | pubmed-author:LawC LCL | lld:pubmed |
| pubmed-article:8657103 | pubmed:author | pubmed-author:ChandranK AKA | lld:pubmed |
| pubmed-article:8657103 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8657103 | pubmed:volume | 16 | lld:pubmed |
| pubmed-article:8657103 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8657103 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8657103 | pubmed:pagination | 1305-15 | lld:pubmed |
| pubmed-article:8657103 | pubmed:dateRevised | 2011-11-2 | lld:pubmed |
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