The role of EGF receptor ubiquitination in regulating its intracellular traffic.
Traffic. 2012 Feb; 13:329-37
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Many receptors are modified by ubiquitination, which has been suggested to play a role in endocytosis. This paper shows that ubiquitination of epidermal growth factor receptor (EGFR) does not affect endocytosis per se but is critical for interaction with endosomal-sorting complex required for transport (ESCRT) component(s) and for EGFR-induced production of intraluminal vesicles (ILV) and the localization of EGFR to the ILV within multivesicular bodies (MVB) for down-regulation.
The authors comes to the conclusion that ubiquitination is required for EGFR entry to ILV by monitoring the behavior of an ubiquitination-defective EGFR mutant (15KR-EGFR) in the cell. In contrast to wild-type EGFR, 15KR-EGFR shows defects in the interaction with and phosphorylation of the Hrs component of the ESCRT complex. In addition, 15KR-EGFR is localized to the limiting membrane of MVB rather than ILV and is more efficiently recycled back to the cell surface, like the transferrin receptor.
This study shed light on the function of receptor ubiquitination in the biogenesis of MVB and cargo-mediated regulation of the endocytic pathway.
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Li G: F1000Prime Recommendation of [Eden ER et al., Traffic 2012, 13:329-37]. In F1000Prime, 16 Dec 2011; DOI: 10.3410/f.13408022.14778136. F1000Prime.com/13408022#eval14778136
F1000Prime Recommendations, Dissents and Comments for [Eden ER et al., Traffic 2012, 13:329-37]. In F1000Prime, 29 Jul 2014; F1000Prime.com/13408022
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