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Originally published In Press as doi:10.1074/jbc.M106428200 on November 15, 2001

J. Biol. Chem., Vol. 277, Issue 4, 2973-2986, January 25, 2002
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PSTPIP Is a Substrate of PTP-PEST and Serves as a Scaffold Guiding PTP-PEST Toward a Specific Dephosphorylation of WASP*

Jean-François CôtéDagger §, Ping Lin ChungDagger , Jean-François Théberge, Maxime HalléDagger ||, Susan Spencer**, Laurence A. Lasky**, and Michel L. TremblayDagger Dagger Dagger

From the Dagger  Department of Biochemistry, McGill University, Montréal, Québec H3G 1Y6, Canada, the  McGill Cancer Center, Montréal, Québec H3G 1Y6, Canada, and the ** Department of Molecular Oncology, Genentech, Inc., South San Francisco, California 94080

PSTPIP is a tyrosine-phosphorylated protein involved in the organization of the cytoskeleton. Its ectopic expression induces filipodial-like membrane extensions in NIH 3T3 cells. We previously observed a defect in cytokinesis and an increase in the tyrosine phosphorylation of PSTPIP in PTP-PEST-deficient fibroblasts. In this article, we demonstrate that PTP-PEST and PSTPIP are found in the same complexes in vivo and that they interact directly through the CTH domain of PTP-PEST and the coiled-coil domain of PSTPIP. We tested pathways that could regulate the tyrosine phosphorylation of PSTPIP. We found that the activation of the epidermal growth factor and platelet-derived growth factor receptors can induce PSTPIP phosphorylation. With the use of the PP2 inhibitor, we demonstrate that Src kinases are not involved in the epidermal growth factor-mediated phosphorylation of PSTPIP. Together with previous results, this suggests that c-Abl is the critical tyrosine kinase downstream of growth factor receptors responsible for PSTPIP phosphorylation. We also demonstrate that PTP-PEST dephosphorylates PSTPIP at tyrosine 344. Importantly, we identified tyrosine 344 as the main phosphorylation site of PSTPIP by performing tryptic phosphopeptide maps. This is an important finding since tyrosine 367 of PSTPIP was also proposed as a candidate phosphorylation site involved in the negative regulation of the association between PSTPIP and WASP. In this respect, we observed that the PSTPIP·WASP complex is stable in vivo and is not affected by the phosphorylation of PSTPIP. Furthermore, we demonstrate that PSTPIP serves as a scaffold protein between PTP-PEST and WASP and allows PTP-PEST to dephosphorylate WASP. This finding suggests a possible mechanism for PTP-PEST to directly modulate actin remodeling through the PSTPIP-WASP interaction.

* This work was supported in part by a grant from the Medical Research Council of Canada (to M. L. T.).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.

§ Research student of the National Cancer Institute of Canada (NCIC) supported with funds provided by the Terry Fox Run and a Canadian Institute of Health and Research (CIHR) post-doctoral fellowship. Present address: The Burnham Institute, 10901 North Torrey Pines Rd., La Jolla, CA 92037. E-mail: jfcote@burnham.org.

|| Recipient of a Fonds pour la Formation de Chercheurs et l'Aide à la Recherche (FCAR) studentship.

Dagger Dagger Scientist of the Medical Research Council of Canada. To whom correspondence should be addressed: McGill Cancer Center, 3655 Sir William Osler Promenade, Rm. 715, McIntyre Medical Sciences Bldg., McGill University, Montréal, Québec H3G 1Y6, Canada. Tel.: 514-398-7290; Fax: 514-398-6769; E-mail: tremblay@med.mcgill.ca.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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