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J. Biol. Chem., Vol. 275, Issue 21, 16219-16226, May 26, 2000
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Site-selective Dephosphorylation of the Platelet-derived Growth Factor beta -Receptor by the Receptor-like Protein-tyrosine Phosphatase DEP-1*

Marina KovalenkoDagger §, Karsten Denner||, Jill SandströmDagger , Camilla PerssonDagger , Steffen Grobeta **, Enrico Jandt, Ramon VilellaDagger Dagger , Frank Böhmer, and Arne ÖstmanDagger §§

From the Dagger  Ludwig Institute for Cancer Research, Box 595, S-751 24, Uppsala, Sweden, the  Molecular Cell Biology Research Unit, Friedrich Schiller University, Drackendorfer Strabeta e 1, D-07747 Jena, Germany, and the Dagger Dagger  Servei d'Immunologia, Hospital Clinic, Villaroel 170, Barcelona 08036, Spain

Ligand stimulation of PDGF beta -receptors leads to autophosphorylation of the regulatory tyrosine 857 and of tyrosine residues that in their phosphorylated form serve as docking sites for Src homology 2 domain-containing proteins. Regulation of the PDGF beta -receptor by protein-tyrosine phosphatases is poorly understood. We have investigated PDGF beta -receptor dephosphorylation by receptor-like protein-tyrosine phosphatase DEP-1 using a cell line with inducible DEP-1 expression and by characterizing in vitro dephosphorylation of the PDGF beta -receptor and of receptor-derived phosphopeptides by DEP-1. After DEP-1 induction PDGF beta -receptor·DEP-1 complexes and reduced receptor tyrosine phosphorylation were observed. Phosphopeptide analysis of the PDGF beta -receptors from DEP-1-expressing cells and of the receptors dephosphorylated in vitro by DEP-1 demonstrated that dephosphorylation of autophosphorylation sites of the receptor differed and revealed that the regulatory Tyr(P)857 was not a preferred site for DEP-1 dephosphorylation. When dephosphorylation of synthetic receptor-derived peptides was analyzed, the selectivity was reproduced, indicating that amino acid sequence surrounding the phosphorylation sites is the major determinant of selectivity. This notion is supported by the observation that the poorly dephosphorylated Tyr(P)562 and Tyr(P)857, in contrast to other analyzed phosphorylation sites, are surrounded by basic amino acid residues at positions -4 and +3 relative to the tyrosine residue. Our study demonstrates that DEP-1 dephosphorylation of the PDGF beta -receptor is site-selective and may lead to modulation, rather than general attenuation, of signaling.

* This work was supported by grants from the Max-Planck-Society (to F. D. B.), Deutsche Forschungsgemeinschaft Grant BO1043/4-1 (to F. D. B.), and a travel grant from Deutscher Akademischer Austauschdienst and the Svenska Institutet (to A. Ö. and 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.

§ Supported in part by a grant from the Wenner-Gren Foundation.

|| Present address: Research Laboratories, Schering AG, 13342 Berlin, Germany.

** Present address: Dept. of Cell Biology and Histology, University of Nijmegen, NL6525-EK Nijmegen, The Netherlands.

§§ To whom correspondence should be addressed. Tel.: 46-18-160414; Fax: 46-18-160420; E-mail: Arne.Ostman@licr.uu.se.

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