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The role of EGF receptor ubiquitination in regulating its intracellular traffic.

Authors
  • Eden, Emily R
  • Huang, Fangtian
  • Sorkin, Alexander
  • Futter, Clare E
Type
Published Article
Journal
Traffic (Copenhagen, Denmark)
Publication Date
Feb 01, 2012
Volume
13
Issue
2
Pages
329–337
Identifiers
DOI: 10.1111/j.1600-0854.2011.01305.x
PMID: 22017370
Source
Medline
License
Unknown

Abstract

Progression of activated EGF receptor (EGFR) through the endocytic pathway regulates EGFR signaling. Here we show that a non-ubiquitinated EGFR mutant, unable to bind the endosomal-sorting complex required for transport (ESCRT) component, Hrs, is not efficiently targeted onto intraluminal vesicles (ILVs) of multivesicular endosomes/bodies (MVBs). Moreover, ubiquitination and ESCRT engagement of activated EGFR are required for EGF-stimulated ILV formation. Non-ubiquitinated EGFRs enter clathrin-coated tubules emanating from MVBs and show enhanced recycling to the plasma membrane, compared to wild-type EGFR.

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