Ubiquitin and Membrane Protein Turnover: From Cradle to Grave

MacGurn, Jason A.; Hsu, Pi-Chiang; Emr, Scott D.

doi:10.1146/annurev-biochem-060210-093619

Cited by 287

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Ubiquitin and Membrane Protein Turnover: From Cradle to Grave

MacGurn, Jason A., Hsu, Pi-Chiang, Emr, Scott D.·2012·Annual Review of Biochemistry

DOI 10.1146/annurev-biochem-060210-093619

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Abstract

From the moment of cotranslational insertion into the lipid bilayer of the endoplasmic reticulum (ER), newly synthesized integral membrane proteins are subject to a complex series of sorting, trafficking, quality control, and quality maintenance systems. Many of these processes are intimately controlled by ubiquitination, a posttranslational modification that directs trafficking decisions related to both the biosynthetic delivery of proteins to the plasma membrane (PM) via the secretory pathway and the removal of proteins from the PM via the endocytic pathway. Ubiquitin modification of integral membrane proteins (or “cargoes”) generally acts as a sorting signal, which is recognized, captured, and delivered to a specific cellular destination via specialized trafficking events. By affecting the quality, quantity, and localization of integral membrane proteins in the cell, defects in these processes contribute to human diseases, including cystic fibrosis, circulatory diseases, and various neuropathies. This review summarizes our current understanding of how ubiquitin modification influences cargo trafficking, with a special emphasis on mechanisms of quality control and quality maintenance in the secretory and endocytic pathways.

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Signaling and internalization of receptors largely depends on recruitment of specific adaptor proteins, including ubiquitin-ligases and epsins.
“Signaling and internalization of receptors largely depends on recruitment of specifi c adaptor proteins, including ubiquitin-ligases and epsins ( 13, 14, 46 ).”
From The LXR-IDOL axis defines a clathrin-, caveolae-, and dynamin-independent endocytic route for LDLR internalization and lysosomal degradation (2013) · cites this paper as [14]

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Authors: MacGurn, J. A., Hsu, P.-C., & Emr, S. D.
Affiliations: Weill Institute for Cell and Molecular Biology, Cornell University, Ithaca, New York 14853;
Venue: Annual Review of Biochemistry
Publisher: Annual Reviews
Published: 2012-07-07
Volume: 81
Issue: 1
Pages: 231-259
ISSN: 0066-4154
1545-4509
DOI: 10.1146/annurev-biochem-060210-093619
Cited by: 287
References: 8
Language: en

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Ubiquitin and Membrane Protein Turnover: From Cradle to Grave

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