Ubiquitination and proteasomal activity is required for transport of the EGF receptor to inner membranes of multivesicular bodies

@article{Longva2002UbiquitinationAP,
  title={Ubiquitination and proteasomal activity is required for transport of the EGF receptor to inner membranes of multivesicular bodies},
  author={Karianne Eide Longva and Fr{\o}ydis D. Blystad and Espen Stang and Astrid M. Larsen and Lene E. Johannessen and Inger Helene Madshus},
  journal={The Journal of Cell Biology},
  year={2002},
  volume={156},
  pages={843 - 854}
}
EGF, but not TGF alpha, efficiently induces degradation of the EGF receptor (EGFR). We show that EGFR was initially polyubiquitinated to the same extent upon incubation with EGF and TGF alpha, whereas the ubiquitination was more sustained by incubation with EGF than with TGF alpha. Consistently, the ubiquitin ligase c-Cbl was recruited to the plasma membrane upon activation of the EGFR with EGF and TGF alpha, but localized to endosomes only upon activation with EGF. EGF remains bound to the… CONTINUE READING

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