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Papers In Press, published online ahead of print March 18, 2004
Cell and Developmental Biology, Graduate School of Biostudies, Kyoto University, Kyoto 606-8502
Corresponding Author: L50174{at}sakura.kudpc.kyoto-u.ac.jp
Src homology 2 containing phospho-tyrosine phosphatase (Shp2) functions as a positive effector in receptor tyrosine kinase (RTK) signaling immediately proximal to activated receptors. However, neither its physiological substrate(s) nor its mechanism of action in RTK signaling has been defined. In this study, we demonstrate that Sprouty (Spry) is a possible target of Shp2. Spry acts as a conserved inhibitor of RTK signaling, and tyrosine phosphorylation of Spry is indispensable for its inhibitory activity. Shp2 was able to dephosphorylate fibroblast growth factor Receptor (FGFR)-induced phospho-tyrosines on Spry both in vivo and in vitro. Shp2-mediated dephosphorylation of Spry resulted in dissociation of Spry from Grb2. Furthermore, Shp2 could reverse the inhibitory effect of Spry on FGF-induced neurite outgrowth and MAP kinase activation. These findings suggest that Shp2 acts as a positive regulator in RTK signaling by dephosphorylating and inactivating Spry.
J. Biol. Chem, 10.1074/jbc.M312498200
Submitted on November 14, 2003
Revised on February 26, 2004
Accepted on March 18, 2004
Shp2, an SH2-containing protein tyrosine phosphatase, positively regulates receptor tyrosine kinase signaling by dephosphorylating and inactivating the inhibitor sprouty
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