Molecular cloning of human paxillin, a focal adhesion protein phosphorylated by P210BCR/ABL.

@article{Salgia1995MolecularCO,
  title={Molecular cloning of human paxillin, a focal adhesion protein phosphorylated by P210BCR/ABL.},
  author={Ravi Salgia and Ji Liang Li and Su Hao Lo and Beatrice Brunkhorst and Geoffrey Scott Kansas and E S Sobhany and Y. Sun and Evan Pisick and Michael J Hallek and Thomas Michael Ernst},
  journal={The Journal of biological chemistry},
  year={1995},
  volume={270 10},
  pages={
          5039-47
        }
}
Paxillin is a 68-kDa focal adhesion protein that is phosphorylated on tyrosine residues in fibroblasts in response to transformation by v-src, treatment with platelet-derived growth factor, or cross-linking of integrins. Paxillin has been shown to have binding sites for the SH3 domain of Src and the SH2 domain of Crk in vitro and to coprecipitate with two other focal adhesion proteins, vinculin and focal adhesion kinase (p125fak). After preliminary studies showed that paxillin was a substrate… CONTINUE READING

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