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Trends Cell Biol. 2011 Nov;21(11):647-55. doi: 10.1016/j.tcb.2011.08.007. Epub 2011 Sep 28.

Endosomal transport via ubiquitination.

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1
Molecular Physiology and Biophysics, University of Iowa, Iowa City, IA 52242, USA. Robert-Piper@uiowa.edu

Abstract

Cell survival, growth, differentiation and homeostasis rely on exquisite control of the abundance of particular cell-surface membrane proteins. Cell-surface proteins must respond appropriately to environmental and intracellular cues, often undergoing regulated internalization and lysosomal degradation. These proteins also can sustain damage and must be recognized and removed. A unifying mechanism has emerged for the trafficking of damaged and downregulated proteins to the lysosome by their attachment to ubiquitin (Ub), which serves as a sorting signal for clathrin-mediated internalization and sorting into late endosomes. Major questions remain as to how this system is governed, how it is adapted for different proteins, and whether Ub serves as more than a one-way ticket to the lysosome for degradation. Here, we highlight recent insights and the challenges that remain.

PMID:
21955996
PMCID:
PMC3225009
DOI:
10.1016/j.tcb.2011.08.007
[Indexed for MEDLINE]
Free PMC Article
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