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Originally published In Press as doi:10.1074/jbc.M102777200 on February 4, 2002

J. Biol. Chem., Vol. 277, Issue 18, 15962-15970, May 3, 2002
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Interaction of Fibroblast Growth Factor Receptor 3 and the Adapter Protein SH2-B
A ROLE IN STAT5 ACTIVATION*

Monica KongDagger , Ching S. WangDagger , and Daniel J. Donoghue§

From the Department of Chemistry and Biochemistry, Center for Molecular Genetics, University of California San Diego, La Jolla, California 92093-0367

Fibroblast growth factor receptor 3 (FGFR3) influences a diverse array of biological processes, including cell growth, differentiation, and migration. Activating mutations in FGFR3 are associated with multiple myeloma, cervical carcinoma, and bladder cancer. To identify proteins that interact with FGFR3 and which may mediate FGFR3-dependent signaling, a yeast two-hybrid screen was employed using the cytoplasmic kinase domain of FGFR3 as bait. We identified the adapter protein SH2-B as an FGFR3-interacting protein. Coimmunoprecipitation experiments demonstrate binding of the SH2-Bbeta isoform to FGFR3 in 293T cells. Tyrosine phosphorylation of SH2-Bbeta was observed when coexpressed with activated FGFR3 mutants such as the weakly activated mutant N540K or the strongly activated mutant K650E, both associated with human developmental syndromes. The extent of tyrosine phosphorylation of SH2-Bbeta correlates with receptor activation, suggesting that FGFR3 activation mediates tyrosine phosphorylation of SH2-Bbeta . Furthermore, two tyrosine phosphorylation sites of FGFR3, Tyr-724 and Tyr-760, are required for optimal binding of the Src homology-2 (SH2) domain of SH2-Bbeta . We also demonstrate the phosphorylation and nuclear translocation of Stat5 by activated FGFR3, which increases in response to overexpression of SH2-Bbeta . Taken together, our results identify SH2-Bbeta as a novel FGFR3 binding partner that mediates signal transduction.

* This work was supported by National Institutes of Health Grant 1R01 DE12581.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 These authors contributed equally to this work.

§ To whom correspondence should be addressed: Dept. of Chemistry and Biochemistry, Center for Molecular Genetics, University of California at San Diego, La Jolla, CA 92093-0367. Tel.: 858-534-2167; Fax: 858-534-7481; E-mail: ddonoghue@ucsd.edu.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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