A mutant EGF‐receptor defective in ubiquitylation and endocytosis unveils a role for Grb2 in negative signaling

@article{Waterman2002AME,
  title={A mutant EGF‐receptor defective in ubiquitylation and endocytosis unveils a role for Grb2 in negative signaling},
  author={H. Waterman and M. Katz and C. Rubin and K. Shtiegman and S. Lavi and A. Elson and T. Jovin and Y. Yarden},
  journal={The EMBO Journal},
  year={2002},
  volume={21}
}
Ligand‐induced desensitization of the epidermal growth factor receptor (EGFR) is controlled by c‐Cbl, a ubiquitin ligase that binds multiple signaling proteins, including the Grb2 adaptor. Consistent with a negative role for c‐Cbl, here we report that defective Tyr1045 of EGFR, an inducible c‐Cbl docking site, enhances the mitogenic response to EGF. Signaling potentiation is due to accelerated recycling of the mutant receptor and a concomitant defect in ligand‐induced ubiquitylation and… Expand
Cbl-dependent ubiquitination is required for progression of EGF receptors into clathrin-coated pits.
Grb2 regulates internalization of EGF receptors through clathrin-coated pits.
EGF receptor ubiquitination is not necessary for its internalization
Abl Tyrosine Kinase Regulates Endocytosis of the Epidermal Growth Factor Receptor*
Association with HSP90 inhibits Cbl-mediated down-regulation of mutant epidermal growth factor receptors.
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