Protein quality control in the ER: balancing the ubiquitin checkbook
Name
Ploegh_Protein quality.pdf
Size
4.14 MB
Format
Adobe PDF
Checksum (MD5)
93a5daaf21e4d61b527bacfa2eaa11bb
Author(s)
Kundrat, Lenka
Ploegh, Hidde
Claessen, Jasper H. L.
Date Issued
November 2011
Journal
Trends in Cell Biology
Publisher
Elsevier
Citation
Claessen, Jasper H.L., Lenka Kundrat, and Hidde L. Ploegh. “Protein Quality Control in the ER: Balancing the Ubiquitin Checkbook.” Trends in Cell Biology 22, no. 1 (January 2012): 22–32.
Version
Author's final manuscript
Abstract
Protein maturation in the endoplasmic reticulum (ER) is subject to stringent quality control. Terminally misfolded polypeptides are usually ejected into the cytoplasm and targeted for destruction by the proteasome. Ubiquitin conjugation is essential for both extraction and proteolysis. We discuss the role of the ubiquitin conjugation machinery in this pathway and focus on the role of ubiquitin ligase complexes as gatekeepers for membrane passage. We then examine the type of ubiquitin modification applied to the misfolded ER protein and the role of de-ubiquitylating enzymes in the extraction of proteins from the ER.
MIT Department
Massachusetts Institute of Technology. Department of Biology
Whitehead Institute for Biomedical Research
Terms of Use
Creative Commons Attribution-Noncommercial-NoDerivatives
Persistent DSpace Link
DOI of Published Version
https://doi.org/10.1016/j.tcb.2011.09.010
