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Originally published In Press as doi:10.1074/jbc.M001315200 on June 1, 2000

J. Biol. Chem., Vol. 275, Issue 34, 26376-26384, August 25, 2000
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The Protein-tyrosine Phosphatase SHP-1 Binds to and Dephosphorylates p120 Catenin*

Heike KeilhackDagger , Ulf Hellman§, Jolanda van Hengel||, Frans van Roy**, Jasminka Godovac-ZimmermannDagger Dagger §§, and Frank-D. BöhmerDagger ¶¶

From the Dagger  Research Unit "Molecular Cell Biology," Klinikum der Friedrich-Schiller-Universität Jena, Drackendorfer Strasse 1, D-07747 Jena, Germany, the § Ludwig Institute for Cancer Research, Uppsala Branch, SE-75124 Uppsala, Sweden, the  Molecular Cell Biology Unit, Department of Molecular Biology, Flanders Interuniversity Institute for Biotechnology, University of Ghent, Ledeganckstraat 35, B-9000 Ghent, Belgium, and the Dagger Dagger  Institute for Molecular Biotechnology, Beutenbergstrasse 11, D-07745 Jena, Germany

A prominent tyrosine-phosphorylated protein of ~100 kDa (designated pp100) in epidermal growth factor (EGF)-stimulated A431 cells was found to be a main interaction partner of the protein-tyrosine phosphatase SHP-1 in pull-down experiments with a glutathione S-transferase-SHP-1 fusion protein. Binding was largely mediated by the N-terminal SH2 domain of SHP-1 and apparently direct and independent from the previously described association of SHP-1 with the activated EGF receptor. pp100 was partially purified and identified by mass spectrometric analysis of tryptic fragments, partial amino acid sequencing, and use of authentic antibodies as the 3A isoform of the Armadillo repeat protein superfamily member p120 catenin (p120ctn). Different p120ctn isoforms expressed in human embryonal kidney 293 cells, exhibited differential binding to SHP-1 that correlated partly with the extent of EGF-dependent p120ctn tyrosine phosphorylation. Despite strong phosphorylation, p120ctn isoforms 3B and 3AB bound, however, less readily to SHP-1. SHP-1 associated transiently with p120ctn in EGF-stimulated A431 cells stably transfected with a tetracycline-responsive SHP-1 expression construct, and p120ctn exhibited elevated phosphorylation upon a tetracycline-mediated decrease in the SHP-1 level. Functions of p120ctn, which are regulated by tyrosine phosphorylation, may be modulated by the described SHP-1-p120ctn interaction.

* This work was supported by Grant Bo 1043/3-1 from the Deutsche Forschungsgemeinschaft (to F.-D. B. and J. G.-Z.) and by a grant from the Max-Planck Society (to F.-D. B.).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.

|| Postdoctoral Fellow of the Fund for Scientific Research, Flanders.

** Research Director of the Fund for Scientific Research, Flanders.

§§ Present address: Centre for Molecular Medicine, University College London, 5 University Street, London WC1E 6JJ, UK.

¶¶ To whom correspondence should be addressed. Fax: 49-3641-304462; E-mail: i5frbo@rz.uni-jena.de.

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