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J Biol Chem, Vol. 273, Issue 29, 17987-17990, July 17, 1998
From the Fibroblast growth factors (FGFs) stimulate
tyrosine phosphorylation of a membrane-anchored adapter protein,
FRS2/SNT-1, promoting its association with Shp-2 tyrosine phosphatase
and upstream activators of Ras. Using the yeast two-hybrid
protein-protein interaction assay, we show that FRS2/SNT-1 and a newly
isolated SNT-2 protein directly bind to FGF receptor-1 (FGFR-1). A
juxtamembrane segment of FGFR-1 and the phosphotyrosine-binding domain
of SNTs are both necessary and sufficient for interaction in yeast and
in vitro, and FGFR-mediated SNT tyrosine phosphorylation
in vivo requires these segments of receptor and SNT. Our
findings establish SNTs as direct protein links between FGFR-1 and
multiple downstream pathways. The SNT binding motif of FGFR-1 is
distinct from previously described phosphotyrosine-binding domain
recognition motifs, lacking both tyrosine and asparagine residues.
COMMUNICATION
Novel Recognition Motif on Fibroblast Growth Factor Receptor
Mediates Direct Association and Activation of SNT Adapter Proteins
§,§, and
Brookdale Center for Developmental and
Molecular Biology and the § Graduate Program in Molecular,
Cellular, Biochemical and Developmental Sciences, Mount Sinai School of
Medicine, New York, New York 10029
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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