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Tyrosine 319 in the interdomain B of ZAP-70 is a binding site for the Src homology 2 domain of Lck.

Abstract:

T-cell antigen receptor-induced signaling requires both ZAP-70 and Lck protein-tyrosine kinases. One essential function of Lck in this process is to phosphorylate ZAP-70 and up-regulate its catalytic activity. We have previously shown that after T-cell antigen receptor stimulation, Lck binds to ZAP-70 via its Src homology 2 (SH2) domain (LckSH2) and, more recently, that Tyr319 of ZAP-70 is phosphorylated in vivo and plays a positive regulatory role. Here, we investigated the possibility that ...

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Publication status:
Published

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Publisher copy:
10.1074/jbc.274.20.14229

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Journal:
Journal of biological chemistry
Volume:
274
Issue:
20
Pages:
14229-14237
Publication date:
1999-05-01
DOI:
EISSN:
1083-351X
ISSN:
0021-9258
Source identifiers:
17164

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