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Originally published In Press as doi:10.1074/jbc.M007478200 on September 15, 2000

J. Biol. Chem., Vol. 275, Issue 50, 39073-39080, December 15, 2000
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Recruitment of the Protein-tyrosine Phosphatase SHP-2 to the C-terminal Tyrosine of the Prolactin Receptor and to the Adaptor Protein Gab2*

Samir AliDagger and Suhad Ali§

From the Department of Medicine, Division of Hematology and Molecular Oncology Group, Royal Victoria Hospital, McGill University, Montreal, Quebec H3A 1A1, Canada

The protein-tyrosine phosphatase SHP-2 modulates signaling events through receptor tyrosine kinases and cytokine receptors including the receptor for prolactin (PRLR). Here we investigated mechanisms of SHP-2 recruitment within the PRLR signaling complex. Using SHP-2 and PRLR immunoprecipitation studies in 293 cells and in the mouse mammary epithelial cell line HC11, we found that SHP-2 co-immunoprecipitates with the PRLR and that the C-terminal tyrosine of the PRLR plays a regulatory role in both the tyrosine phosphorylation and the recruitment of SHP-2. Our results further indicate that SHP-2 association to the PRLR occurs via the C-terminal SH2 domain of the phosphatase. In addition, we determined that the newly identified adaptor protein Gab2, but not Gab1, is specifically tyrosine phosphorylated and is able to recruit SHP-2 and phosphatidyinositol 3-kinase in response to PRLR activation. Together, these studies suggest the presence of dual recruitment sites for SHP-2; the first is to the C-terminal tyrosine of the PRLR and the second is to the adaptor protein Gab2.

* This work was supported by Medical Research Council of Canada Grant MOP-13681 (to Su. A.).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 Recipient of the Fonds de la Recherche en Santé du Québec Studentship Award.

§ Fonds de la Recherche en Santé du Québec scholar. To whom correspondence should be addressed: Royal Victoria Hospital, Molecular Oncology Group, H5-81, 687 Pine Ave. West, Montreal, PQ H3A 1A1, Canada. Tel.: 514-842-1231, Ext. 4863; Fax: 514-843-1478: E-mail: Suhad.Ali@muhc.mcgill.ca.

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