HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Tsuchida, M. Articles by Hamawy, M. M. Search for Related Content PubMed PubMed Citation Articles by Tsuchida, M. Articles by Hamawy, M. M. Social Bookmarking                      What's this?

J Biol Chem, Vol. 275, Issue 2, 1344-1350, January 14, 2000

Regulation of T Cell Receptor- and CD28-induced Tyrosine Phosphorylation of the Focal Adhesion Tyrosine Kinases Pyk2 and Fak by Protein Kinase C
A ROLE FOR PROTEIN TYROSINE PHOSPHATASES^*

Masahiro Tsuchida, Eric R. Manthei, Tausif Alam, Stuart J. Knechtle, and Majed M. Hamawy

From the Department of Surgery, University of Wisconsin, Madison, Wisconsin 53792

The T cell receptor (TCR)-CD3 complex and the costimulatory molecule CD28 are critical for T cell function. Both receptors utilize protein tyrosine kinases (PTKs) for the phosphorylation of various signaling molecules, a process that is critical for the function of both receptors. The PTKs of the focal adhesion family, Pyk2 and Fak, have been implicated in the signaling of TCR and CD28. We show here evidence for the regulation of TCR- and CD28-induced tyrosine phosphorylation of the focal adhesion PTKs by protein kinase C (PKC). Thus, treating Jurkat T cells with the PKC activator phorbol 12-myristate 13-acetate (PMA) rapidly and strongly reversed receptor-induced tyrosine phosphorylation of the focal adhesion PTKs. In contrast, PMA did not affect TCR-induced tyrosine phosphorylation of CD3 or the PTKs Fyn and Zap-70. However, PMA induced a strong and rapid dephosphorylation of the linker molecule for activation of T cells. PMA failed to induce the dephosphorylation of proteins in PKC-depleted cells or in cells pretreated with the PKC inhibitor Ro-31-8220, confirming the role of PKC in mediating the PMA effect on receptor-induced protein tyrosine phosphorylation. The involvement of protein tyrosine phosphatases (PTPases) in mediating the dephosphorylation of the focal adhesion PTKs was confirmed by the failure of PMA to dephosphorylate Pyk2 in cells pretreated with the PTPase inhibitor orthovanadate. These results implicate PKC in the regulation of receptor-induced tyrosine phosphorylation of the focal adhesion PTKs in T cells. The data also suggest a role for PTPases in the PKC action.

CiteULike

Complore

Connotea

Del.icio.us

Digg

Reddit

Technorati

This article has been cited by other articles:

				B. Butler and S. D. Blystone Tyrosine Phosphorylation of {beta}3 Integrin Provides a Binding Site for Pyk2 J. Biol. Chem., April 15, 2005; 280(15): 14556 - 14562. [Abstract] [Full Text] [PDF]

				L. Y. Romanova, S. Hashimoto, K.-O. Chay, M. V. Blagosklonny, H. Sabe, and J. F. Mushinski Phosphorylation of paxillin tyrosines 31 and 118 controls polarization and motility of lymphoid cells and is PMA-sensitive J. Cell Sci., August 1, 2004; 117(17): 3759 - 3768. [Abstract] [Full Text] [PDF]

				P. Maher How Protein Kinase C Activation Protects Nerve Cells from Oxidative Stress-Induced Cell Death J. Neurosci., May 1, 2001; 21(9): 2929 - 2938. [Abstract] [Full Text] [PDF]