Hypophosphorylation of residue Y1045 leads to defective downregulation of EGFRvIII

@article{Han2006HypophosphorylationOR,
  title={Hypophosphorylation of residue Y1045 leads to defective downregulation of EGFRvIII},
  author={Wei Han and Tao Zhang and Hong Yu and John Foulke and Careen K. Tang},
  journal={Cancer Biology \& Therapy},
  year={2006},
  volume={5},
  pages={1361 - 1368}
}
Down-regulation of the EGF receptor is the net result of receptor degradation and recycling. Cbl functions by specifically targeting activated ErbB receptors for ubiquitination, facilitating ligand-induced desensitization of EGFR. The interaction between EGFR and c-Cbl has been shown to depend upon receptor phosphorylation at tyrosine residue 1045, the major docking site for c-Cbl. To better understand the biological consequences of EGFR mutants in human cancers, we compared wild-type EGFR and… Expand
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