Sh. Ong et al., SHP2 ASSOCIATES DIRECTLY WITH TYROSINE-PHOSPHORYLATED P90 (SNT) PROTEIN IN FGF-STIMULATED CELLS, Biochemical and biophysical research communications, 238(1), 1997, pp. 261-266
In a number of cell lines responsive to basic fibroblast growth factor
(bFGF), two major tyrosine phosphorylated proteins, of molecular weig
hts around 120kDa and 90kDa, are precipitated. along with the tyrosine
phosphatase SHP2 from the lysates of stimulated cells, The docker pro
tein Gab-1 represents at least part of the 120kDa protein(s). The p90
protein was identified as the SNT protein, The two SH2 domains of SHP2
bind directly and synergistically to tyrosine phosphorylated SNT. Tyr
osine phosphorylated SNT does not bind SHP1 and does riot appear to be
an in vivo substrate of SHP2 but is likely to function as an adapter
protein in FGF-signalling. (C) 1997 Academic Press.