Involvement of EphA2-mediated tyrosine phosphorylation of Shp2 in Shp2-regulated activation of extracellular signal-regulated kinase

@article{Miura2013InvolvementOE,
  title={Involvement of EphA2-mediated tyrosine phosphorylation of Shp2 in Shp2-regulated activation of extracellular signal-regulated kinase},
  author={Kunio Miura and Yuki Wakayama and Mishie Ann Tanino and Yasuko Orba and H Sawa and M{\'a}rcia Hatakeyama and Shinya Tanaka and H. Sabe and Naoki Mochizuki},
  journal={Oncogene},
  year={2013},
  volume={32},
  pages={5292-5301}
}
Shp2 is a positive regulator for Erk activation downstream of receptor tyrosine kinases for growth factors. It has been controversial how Shp2 induces Erk activation. We here demonstrate that EphA2 is responsible for Shp2-mediated Erk activation by phosphorylating Tyr542 and Tyr580 of Shp2 in the cells stimulated with growth factors. In NMuMG mammary epithelial cells stimulated with hepatocyte growth factor (HGF), HGF-dependent Erk phosphorylation was prolonged only in the presence of EphA2… CONTINUE READING