A tyrosine-phosphorylated 70-kDa protein binds a photoaffinity analogue of ATP and associates with both the ζ chain and CD3 components of the activated T cell antigen receptor

Ronald L. Wange, Ah-Ng Kong, Lawrence E. Samelson

Research output: Contribution to journalArticle

111 Scopus citations

Abstract

An early event in T cell antigen receptor (TCR)-mediated signal transduction is the activation of a protein tyrosine kinase (PTK) pathway. An unidentified PTK activity and a kinase substrate termed ZAP-70 have previously been shown to associate with TCRζ upon cross-linking of TCRβ. Here we report that TCR activation, by antibody cross-linking of either TCRβ or CD3∈, results in the association of a PTK activity with both CD3 and TCRζ. A number of in vitro PTK substrates are also associated with CD3 and TCRζ, including CD3∈, TCRζ, p60fyn, p62yes, and a predominant 70-kDa protein (ZAP-70). The shared PTK activity and PTK substrates suggest that both CD3 and TCRζ are involved in signal transduction via a shared pathway. We used [α-32P]γ-azidoanilido ATP, a photoreactive analogue of ATP, to detect CD3-associated proteins that bound ATP upon TCR activation, reasoning that such proteins could represent PTKs. A 70-kDa protein bound [α-32P]γ-azidoanilido ATP only upon TCR activation, and we propose that this protein and the 70-kDa PTK substrate are the same protein. Furthermore, we propose that this protein is responsible for the PTK activity observed to be associated with TCRζ and CD3 upon TCR activation.

Original languageEnglish (US)
Pages (from-to)11685-11688
Number of pages4
JournalJournal of Biological Chemistry
Volume267
Issue number17
StatePublished - Jun 15 1992
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biochemistry

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