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J Biol Chem, Vol. 275, Issue 5, 3391-3396, February 4, 2000

The Carboxyl-terminal Tyrosine Residue of Protein-tyrosine Phosphatase alpha  Mediates Association with Focal Adhesion Plaques*

Reiner LammersDagger , Markus M. Lerch§, and Axel Ullrich

From the Max-Planck-Institut für Biochemie, Am Klopferspitz 18A, D-82152 Martinsried, Germany

The receptor protein-tyrosine phosphatase alpha  (PTPalpha ) is involved in the activation of c-Src kinase as well as in down-regulation of the insulin signal. To investigate the role of PTPalpha in activation of the Src kinase in more detail we tried to overexpress this phosphatase in NIH3T3 fibroblasts. Although PTPalpha has been overexpressed in rat embryonic fibroblasts and in embryonic carcinoma cells and should increase mitogenic responses we were not able to achieve a detectable overexpression. In contrast, expression of partially (C442S) or completely inactive (C442S,C732S) PTPalpha or of phosphatase active PTPalpha containing mutation Y781F or Y798F was possible. The level of expression, however, was reduced to background after several passages of lines expressing PTPalpha C442S,C732S and PTPalpha Y781F. When employed in a focus formation assay, only infection with virus encoding PTPalpha Y798F induced Src-dependent formation of foci. In immunofluorescence studies, PTPalpha C442S and PTPalpha Y781F but not PTPalpha Y798F colocalized with proteins found in focal adhesion plaques. Treatment of PTPalpha C442S-overexpressing cells with vanadate abolished this colocalization and led to proteolytic processing of the phosphatase. We conclude that tyrosine 798 in PTPalpha is important for localization at focal adhesion plaques. Inhibition of phosphatases by vanadate treatment releases PTPalpha from focal adhesions.

* 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 Present address: Medizinische Klinik IV, Eberhard-Karls-Universität, Otfried-Müller Strasse 10, D-72076 Tübingen, Germany. To whom correspondence should be addressed. Tel.: 49-7071-298-7599; Fax: 49-7071-295-974; E-mail: rrlammer@med.uni-tuebingen.de.

§ Present address: Medizinische Klinik B, Westfälische Wilhelms-Universität, Albert-Schweizer Strasse 33, D-48129 Münster, Germany.

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