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J Biol Chem, Vol. 275, Issue 19, 14590-14597, May 12, 2000

Evidence That Lck-mediated Phosphorylation of p56dok and p62dok May Play a Role in CD2 Signaling*

Jean-Guy Némorin and Pascale DuplayDagger

From the Institut National de la Recherche Scientifique, Institut Armand-Frappier, Université du Québec, Laval, Québec H7V 1B7, Canada

The Lck tyrosine kinase is involved in signaling by T cell surface receptors such as TCR/CD3, CD2, and CD28. As other downstream protein-tyrosine kinases are activated upon stimulation of these receptors, it is difficult to assign which tyrosine-phosphorylated proteins represent bona fide Lck substrates and which are phosphorylated by other tyrosine kinases. We have developed a system in which Lck can be activated independently of TCR/CD3. We have shown that activation of an epidermal growth factor receptor/Lck chimera leads to the specific phosphorylation of Ras GTPase-activating protein (RasGAP) and two RasGAP-associated proteins, p56dok and p62dok. Activation of the chimeric protein correlates with an increase in cellular Ca2+ in the absence of ZAP-70 and phospholipase Cgamma 1 phosphorylation. Furthermore, we have found that p62dok co-immunoprecipitates with the activated epidermal growth factor receptor/LckF505 and that phosphorylated Dok proteins bind to the Src homology 2 domain of Lck in vitro. In addition, we have shown that activation via the CD2 but not the TCR/CD3 receptor leads to the phosphorylation of p56dok and p62dok. Using JCaM1.6 cells, we have demonstrated that Lck is required for CD2-mediated phosphorylation of Dok proteins. We propose that phosphorylation and Src homology 2-mediated association of p56dok and p62dok with Lck play a selective function in accessory receptor signal transduction mechanisms.

* This work was supported by Grant MT-14811 from the Medical Research Council of Canada.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger To whom correspondence should be addressed: Institut National de la Recherche Scientifique, Institut Armand-Frappier, Université du Québec, 531 Boulevard des Prairies, Laval Québec, H7V 1B7, Canada. Tel.: 450-687-5010; Fax: 450-686-5501; E-mail: pascale_duplay@ inrs-iaf.uquebec.ca.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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