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J Biol Chem, Vol. 274, Issue 20, 14229-14237, May 14, 1999
From the 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 Tyr319 mediates the
SH2-dependent interaction between Lck and ZAP-70. We show
that a phosphopeptide encompassing the motif harboring Tyr319, YSDP, interacted with LckSH2, although with a lower
affinity compared with a phosphopeptide containing the optimal binding motif, YEEI. Moreover, mutation of Tyr319 to phenylalanine
prevented the interaction of ZAP-70 with LckSH2. Based on these
results, a gain-of-function mutant of ZAP-70 was generated by changing
the sequence Y319SDP into Y319EEI. As a result
of its increased ability to bind LckSH2, this mutant induced a dramatic
increase in NFAT activity in Jurkat T-cells, was hyperphosphorylated,
and displayed a higher catalytic activity compared with wild-type
ZAP-70. Collectively, our findings indicate that
Tyr319-mediated binding of the SH2 domain of Lck is crucial
for ZAP-70 activation and consequently for the propagation of the
signaling cascade leading to T-cell activation.
Tyrosine 319 in the Interdomain B of ZAP-70 Is a Binding Site
for the Src Homology 2 Domain of Lck
,,,,,,
Molecular Immunology Unit and the ** Cellular
Biochemistry Unit, Institut Pasteur, 25-28 Rue du Docteur Roux, 75724 Paris Cedex 15, France
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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