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J Biol Chem, Vol. 274, Issue 10, 6285-6294, March 5, 1999
From the Following T cell antigen receptor (TCR)
engagement, the protein tyrosine kinase (PTK) ZAP-70 is rapidly
phosphorylated on several tyrosine residues, presumably by two
mechanisms: an autophosphorylation and a trans-phosphorylation by the
Src-family PTK Lck. These events have been implicated in both positive
and negative regulation of ZAP-70 activity and in coupling this PTK to
downstream signaling pathways in T cells. We show here that
Tyr315 and Tyr319 in the interdomain B of
ZAP-70 are autophosphorylated in vitro and become
phosphorylated in vivo upon TCR triggering. Moreover, by
mutational analysis, we demonstrate that phosphorylation of Tyr319 is required for the positive regulation of ZAP-70
function. Indeed, overexpression in Jurkat cells and in a murine T cell
hybridoma of a ZAP-70 mutant in which Tyr319 was replaced
by phenylalanine (ZAP-70-Y319F) dramatically impaired anti-TCR-induced
activation of the nuclear factor of activated T cells and interleukin-2
production, respectively. Surprisingly, an analogous mutation of
Tyr315 had little or no effect. The inhibitory effect of
ZAP-70-Y319F correlated with a substantial loss of its
activation-induced tyrosine phosphorylation and up-regulation of
catalytic activity, as well as with a decreased in vivo
capacity to phosphorylate known ZAP-70 substrates, such as SLP-76 and LAT.
Collectively, our data reveal the pivotal role of Tyr319
phosphorylation in the positive regulation of ZAP-70 and in
TCR-mediated signaling.
Tyrosine 319, a Newly Identified Phosphorylation Site of ZAP-70,
Plays a Critical Role in T Cell Antigen Receptor Signaling
,,,,,,
Molecular Immunology Unit, Department of
Immunology, Institut Pasteur, 25 Rue du Docteur Roux, 75724 Paris
Cedex 15, France and the ¶ Department of Biology, Pharmacia & Upjohn, Viale Pasteur 10, 20014 Nerviano (Milan), Italy
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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