Signaling by tyrosine kinase receptors is mediated by selective interactions between individual Src homology 2 (SH2) domains of cytoplasmic effectors and specific phosphotyroslne residues In the activated recep tor. Here, we report the existence in the hepatocyte growth factor/scatter factor (HGFBF) receptor of a multifunctional docking site made of the tandemly arranged degenerate sequence YVHINV. Phosphoryiation of this site mediates Intermediate-to high-affinity interactions with multiple SHP-contalnlng signal transducers, including phoephatkfylinosftol Skinase, phospholipase CT, ppGP”, and the ORB-~-SOS complex. Mutation of the two tyroslnes results in loss of biological function, as shown by abrogation of the transforming activity in the oncogenic counterpart of the receptor. The same bidentate motif is conserved in the evolutionarlly related receptors Sea and Ron, suggesting that in all members of the HGFlSF receptor family, signal transduction is channeled through a multifunctional binding site.