Heterodimerization of epidermal growth factor receptor and wild-type or kinase-deficient Neu: a mechanism of interreceptor kinase activation and transphosphorylation.

@article{Qian1994HeterodimerizationOE,
  title={Heterodimerization of epidermal growth factor receptor and wild-type or kinase-deficient Neu: a mechanism of interreceptor kinase activation and transphosphorylation.},
  author={Xiang zhong Qian and Charles M LeVea and Jonathan King Freeman and William C. Dougall and M ichael Greene},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1994},
  volume={91 4},
  pages={1500-4}
}
We have shown that members of the erbB family undergo homodimer and heterodimer formation. The rat p185c-neu and the epidermal growth factor receptor (EGFR) can associate into an active heterodimeric tyrosine kinase. Overexpression of these two receptors also results in a transformed phenotype. We now show that mutant Neu proteins resulting from a point mutation at the ATP-binding site (N757) or cytoplasmic domain deletions (N691stop) are still able to undergo EGF-induced heterodimerization… CONTINUE READING
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