Differential signaling after beta1 integrin ligation is mediated through binding of CRKL to p120(CBL) and p110(HEF1).

@article{Sattler1997DifferentialSA,
  title={Differential signaling after beta1 integrin ligation is mediated through binding of CRKL to p120(CBL) and p110(HEF1).},
  author={Martin Sattler and Ravi Salgia and Gautam Shrikhande and Suzie Verma and Naoki Uemura and Susan F Law and Erica A Golemis and James D Griffin},
  journal={The Journal of biological chemistry},
  year={1997},
  volume={272 22},
  pages={14320-6}
}
CRKL is an SH2-SH3-SH3 adapter protein that is a major substrate of the BCR/ABL oncogene. The function of CRKL in normal cells is unknown. In cells transformed by BCR/ABL we have previously shown that CRKL is associated with two focal adhesion proteins, tensin and paxillin, suggesting that CRKL could be involved in integrin signaling. In two hematopoietic cell lines, MO7e and H9, we found that CRKL rapidly associates with tyrosine-phosphorylated proteins after cross-linking of beta1 integrins… CONTINUE READING