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pubmed-article:1717999pubmed:abstractTextStimulation of the T-cell antigen receptor (TCR) leads to tyrosine phosphorylation of a number of cellular proteins, including phospholipase C (PLC) gamma 1 and the TCR zeta chain. We describe here a 70-kDa tyrosine phosphoprotein (ZAP-70) that associates with zeta within 15 sec following TCR stimulation. The phosphorylation of ZAP-70 and its association with zeta is independent of the other TCR chains since stimulation of a functional CD8/zeta chimeric receptor in a TCR-negative T cell leads to coprecipitation of ZAP-70 with the chimeric protein. In a Jurkat cell expressing the TCR and the CD8/zeta chimeric protein, tyrosine phosphorylation and association of ZAP-70 occurs exclusively with the stimulated receptor complex. In addition, a tyrosine kinase that does not appear to be fyn associates with the cytoplasmic domain of zeta and phosphorylates zeta and ZAP-70 in vitro.lld:pubmed
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pubmed-article:1717999pubmed:articleTitleThe zeta chain is associated with a tyrosine kinase and upon T-cell antigen receptor stimulation associates with ZAP-70, a 70-kDa tyrosine phosphoprotein.lld:pubmed
pubmed-article:1717999pubmed:affiliationDivision of Rheumatology, Howard Hughes Medical Institute, University of California, San Francisco 94143.lld:pubmed
pubmed-article:1717999pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:1717999pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
pubmed-article:1717999pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed