Novel recognition motif on fibroblast growth factor receptor mediates direct association and activation of SNT adapter proteins

Hong Xu, Kyung W. Lee, Mitchell Goldfarb

Research output: Contribution to journalArticlepeer-review

150 Scopus citations

Abstract

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.

Original languageEnglish
Pages (from-to)17987-17990
Number of pages4
JournalJournal of Biological Chemistry
Volume273
Issue number29
DOIs
StatePublished - 17 Jul 1998

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