Protein-tyrosine Phosphatase 1D Modulates Its Own State of Tyrosine Phosphorylation (*)
- From the Department of Molecular Biology, Max-Planck-Institute for Biochemistry, Am Klopferspitz 18A, 82152 Martinsried, Germany
- ↵¶ To whom all correspondence should be addressed. Tel.: 49-89-8578-2513 (ext. 2778); Fax: 49-89-857-7866.
Abstract
The insulin receptor-mediated signal transduction pathway involves insulin receptor substrate 1 and a variety of proteins containing Src homology-2 (SH2) domains, such as phosphatidylinositol 3-kinase, Grb2, and protein-tyrosine phosphatase 1D (PTP1D). Upon insulin stimulation of baby hamster kidney cells overexpressing the IR, the catalytically inactive mutant of PTP1D, C463A, becomes tyrosine-phosphorylated and coprecipitates with Grb2. Tyrosine phosphorylation of this mutant is significantly reduced when wild type PTP1D is coexpressed. Substitution of tyrosine residues 546 and 584 with phenylalanine abrogates tyrosine phosphorylation of the catalytically inactive mutant and abolishes its interaction with Grb2.
Footnotes
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↵§ These two authors made an equal contribution to this work.
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↵* This work was supported by a grant from Sugen, Inc. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore by hereby marked “advertisement” in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.
- Received July 7, 1995.
- Revision received August 25, 1995.
- © 1995 by The American Society for Biochemistry and Molecular Biology, Inc.
