Paxillin alpha and Crk-associated substrate exert opposing effects on cell migration and contact inhibition of growth through tyrosine phosphorylation.

@article{Yano2000PaxillinAA,
  title={Paxillin alpha and Crk-associated substrate exert opposing effects on cell migration and contact inhibition of growth through tyrosine phosphorylation.},
  author={Hajime Yano and Hiroshi Uchida and Takanori Iwasaki and Mutsuko Mukai and Hitoshi Akedo and Koji Nakamura and Shu Hashimoto and H. Sabe},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2000},
  volume={97 16},
  pages={9076-81}
}
Protein tyrosine phosphorylation accompanies and is essential for integrin signaling. We have shown that tyrosine phosphorylation of paxillin alpha and Crk-associated substrate (p130(Cas)) is a prominent event on integrin activation in normal murine mammary gland epithelial cells. Tyrosine phosphorylation of p130(Cas) has been demonstrated to facilitate cell migration. We show here that tyrosine phosphorylation of paxillin alpha acts to reduce haptotactic cell migrations as well as… CONTINUE READING
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