A novel phosphotyrosine-binding domain in the N-terminal transforming region of Cbl interacts directly and selectively with ZAP-70 in T cells.

@article{Lupher1996ANP,
  title={A novel phosphotyrosine-binding domain in the N-terminal transforming region of Cbl interacts directly and selectively with ZAP-70 in T cells.},
  author={Mark L. Lupher and Kris A. Reedquist and Satoshi Miyake and Wallace Y Langdon and Hamid Band},
  journal={The Journal of biological chemistry},
  year={1996},
  volume={271 39},
  pages={24063-8}
}
The protooncogene product Cbl has emerged as a novel signal transduction protein downstream of a number of cell surface receptors coupled to tyrosine kinases. Recently, we and others have reported the activation-dependent association of Cbl with the Syk and ZAP-70 tyrosine kinases through presently undefined mechanisms. Potential Src homology 2 and 3 domain binding sites within the C-terminal half of Cbl mediate in vivo interactions with several signaling proteins; however, the N-terminal… CONTINUE READING

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