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J Biol Chem, Vol. 275, Issue 2, 1405-1413, January 14, 2000

The Noncatalytic Domain of Protein-tyrosine Phosphatase-PEST Targets Paxillin for Dephosphorylation in Vivo*

Yu ShenDagger , Patrick LyonsDagger , Marion CooleyDagger , Dominique Davidson§, André Veillette§, Ravi Salgiapar , James D. Griffinpar , and Michael D. SchallerDagger **Dagger Dagger

From the Dagger  Department of Cell Biology & Anatomy and the ** Lineberger Comprehensive Cancer Center, University of North Carolina, Chapel Hill, North Carolina 27599, the § McGill Cancer Centre, McGill University, Montreal, Quebec H3G 1Y6, Canada, and the par  Division of Hematologic Malignancies, Dana Farber Cancer Institute, Boston, Massachusetts 02115

The noncatalytic domain of protein-tyrosine phosphatase (PTP)-PEST contains a binding site for the focal adhesion-associated protein paxillin. This binding site has been narrowed to a 52-residue sequence that is composed of two nonoverlapping, weak paxillin binding sites. The PTP-PEST binding site on paxillin has been mapped to the two carboxyl-terminal LIM (lin11, isl-1, and mec-3) domains. Transient expression of PTP-PEST reduced tyrosine phosphorylation of p130cas, as anticipated. A PTP-PEST mutant defective for binding p130cas does not cause a reduction in its tyrosine phosphorylation in vivo. Expression of PTP-PEST also caused a reduction of phosphotyrosine on paxillin. Expression of mutants of PTP-PEST with deletions in the paxillin-binding site did not associate with paxillin in vivo and failed to cause a reduction in the phosphotyrosine content of paxillin. These results demonstrate that paxillin can serve as a PTP-PEST substrate in vivo and support the model that a noncatalytic domain interaction recruits paxillin to PTP-PEST to facilitate its dephosphorylation.

* This project was supported by National Institutes of Health Grants GM53666 and GM57943 (to M. D. S.).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.

A Senior Scientist of the Medical Research Council of Canada.

Dagger Dagger To whom correspondence should be addressed: Dept. of Cell Biology & Anatomy, Taylor Hall CB 7090, University of North Carolina, Chapel Hill, NC 27599. Tel.: 919-966-0391; Fax: 919-966-1856: E-mail: crispy4@med.unc.edu.

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