| pubmed-article:7539035 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7539035 | lifeskim:mentions | umls-concept:C1705831 | lld:lifeskim |
| pubmed-article:7539035 | lifeskim:mentions | umls-concept:C1527940 | lld:lifeskim |
| pubmed-article:7539035 | lifeskim:mentions | umls-concept:C0034790 | lld:lifeskim |
| pubmed-article:7539035 | lifeskim:mentions | umls-concept:C1421567 | lld:lifeskim |
| pubmed-article:7539035 | lifeskim:mentions | umls-concept:C0108779 | lld:lifeskim |
| pubmed-article:7539035 | lifeskim:mentions | umls-concept:C0271510 | lld:lifeskim |
| pubmed-article:7539035 | lifeskim:mentions | umls-concept:C1332714 | lld:lifeskim |
| pubmed-article:7539035 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
| pubmed-article:7539035 | lifeskim:mentions | umls-concept:C0086597 | lld:lifeskim |
| pubmed-article:7539035 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:7539035 | lifeskim:mentions | umls-concept:C1719914 | lld:lifeskim |
| pubmed-article:7539035 | lifeskim:mentions | umls-concept:C2828406 | lld:lifeskim |
| pubmed-article:7539035 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:7539035 | pubmed:dateCreated | 1995-6-23 | lld:pubmed |
| pubmed-article:7539035 | pubmed:abstractText | During antigen recognition by T cells, CD4 and the T-cell receptor (TCR)/CD3/zeta complex are thought to interact with the same major histocompatibility complex II molecule in a stable ternary complex. Evidence has suggested that the association of CD4 with TCR/CD3/zeta requires the interaction of the protein tyrosine kinase p56lck with CD4. We have taken a biochemical approach to understand the mechanism by which p56lck and, in particular, its src homology (SH) 2 domain contributes to the association of CD4 with TCR/CD3/zeta during activation. We have previously shown that the p56lck SH2 domain binds directly to tyrosine-phosphorylated ZAP-70. Here we formally demonstrate the in vivo association of p56lck with the homologous protein tyrosine kinases Syk and ZAP-70 after CD3 stimulation of Jurkat cells. A tyrosine-phosphorylated peptide containing the sequence predicted to be optimal for binding to the SH2 domain of src family kinases specifically competes for this association, indicating that tyrosine-phosphorylated ZAP-70 and Syk bind to p56lck by an SH2-mediated interaction. We also show that the same peptide is able to compete for the activation-dependent TCR/CD4 association in Jurkat cells. Moreover, ZAP-70 and CD4 cocap only after CD3 stimulation in human T lymphoblasts. We propose that the interaction of the p56lck SH2 domain with zeta-associated tyrosine-phosphorylated ZAP-70 and/or Syk enables CD4 to associate with antigen-stimulated TCR/CD3/zeta complexes. | lld:pubmed |
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| pubmed-article:7539035 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7539035 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7539035 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:7539035 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:7539035 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7539035 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:7539035 | pubmed:issn | 0022-1007 | lld:pubmed |
| pubmed-article:7539035 | pubmed:author | pubmed-author:AcutoOO | lld:pubmed |
| pubmed-article:7539035 | pubmed:author | pubmed-author:ThomeMM | lld:pubmed |
| pubmed-article:7539035 | pubmed:author | pubmed-author:GuttingerMM | lld:pubmed |
| pubmed-article:7539035 | pubmed:author | pubmed-author:DuplayPP | lld:pubmed |
| pubmed-article:7539035 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7539035 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:7539035 | pubmed:volume | 181 | lld:pubmed |
| pubmed-article:7539035 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7539035 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7539035 | pubmed:pagination | 1997-2006 | lld:pubmed |
| pubmed-article:7539035 | pubmed:dateRevised | 2011-11-2 | lld:pubmed |
| pubmed-article:7539035 | pubmed:meshHeading | pubmed-meshheading:7539035-... | lld:pubmed |
