MAP kinase phosphorylation of mSos1 promotes dissociation of mSos1-Shc and mSos1-EGF receptor complexes.

@article{RozakisAdcock1995MAPKP,
  title={MAP kinase phosphorylation of mSos1 promotes dissociation of mSos1-Shc and mSos1-EGF receptor complexes.},
  author={Maria Rozakis-Adcock and Peter van der Geer and Geraldine M. Mbamalu and Tony J. Pawson},
  journal={Oncogene},
  year={1995},
  volume={11 7},
  pages={1417-26}
}
The mouse protein mSos1 has a central Ras guanine nucleotide exchange domain, and a long proline-rich C-terminal tail which contains several potential binding sites for the SH3 domains of the adaptor protein, Grb2. In fibroblasts, growth factor stimulation results in the recruitment of Grb2-mSos1 into complexes with activated receptors and cytoplasmic phosphoproteins such as Shc, which are apparently involved in Ras activation, and subsequently to an increase in mSos1 phosphorylation on serine… CONTINUE READING