A complex of Grb2 adaptor protein, Sos exchange factor, and a 36-kDa membrane-bound tyrosine phosphoprotein is implicated in ras activation in T cells.

@article{Buday1994ACO,
  title={A complex of Grb2 adaptor protein, Sos exchange factor, and a 36-kDa membrane-bound tyrosine phosphoprotein is implicated in ras activation in T cells.},
  author={L{\'a}szl{\'o} Buday and Sean E. Egan and P Rodriguez Viciana and Doreen A Cantrell and Julian Downward},
  journal={The Journal of biological chemistry},
  year={1994},
  volume={269 12},
  pages={9019-23}
}
T lymphocytes contain both Grb2, an SH2 and SH3 domain containing adaptor protein, and Sos, a guanine nucleotide exchange factor for Ras. Immunoprecipitates of Sos from the lysates of T cells contain a 36-kDa protein which is phosphorylated on tyrosine residues in response to T cell receptor/CD3 cross-linking. In vitro studies using different bacterially synthesized GST-Sos fusion proteins confirm the formation of complexes containing p36 and the proline-rich COOH-terminal domain of Sos. The… CONTINUE READING

Citations

Publications citing this paper.
Showing 1-10 of 13 extracted citations

Similar Papers

Loading similar papers…