Please use this identifier to cite or link to this item: https://doi.org/10.1371/journal.pone.0232755
Title: The degradation-promoting roles of deubiquitinases Ubp6 and Ubp3 in cytosolic and ER protein quality control
Authors: Wu, H. 
Ng, D.T.W. 
Cheong, I. 
Matsudaira, P. 
Issue Date: 2020
Publisher: Public Library of Science
Citation: Wu, H., Ng, D.T.W., Cheong, I., Matsudaira, P. (2020). The degradation-promoting roles of deubiquitinases Ubp6 and Ubp3 in cytosolic and ER protein quality control. PLoS ONE 15 (5) : e0232755. ScholarBank@NUS Repository. https://doi.org/10.1371/journal.pone.0232755
Rights: Attribution 4.0 International
Abstract: The quality control of intracellular proteins is achieved by degrading misfolded proteins which cannot be refolded by molecular chaperones. In eukaryotes, such degradation is handled primarily by the ubiquitin-proteasome system. However, it remained unclear whether and how protein quality control deploys various deubiquitinases. To address this question, we screened deletions or mutation of the 20 deubiquitinase genes in Saccharomyces cerevisiae and discovered that almost half of the mutations slowed the removal of misfolded proteins whereas none of the remaining mutations accelerated this process significantly. Further characterization revealed that Ubp6 maintains the level of free ubiquitin to promote the elimination of misfolded cytosolic proteins, while Ubp3 supports the degradation of misfolded cytosolic and ER luminal proteins by different mechanisms. © 2020 Wu et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
Source Title: PLoS ONE
URI: https://scholarbank.nus.edu.sg/handle/10635/199212
ISSN: 1932-6203
DOI: 10.1371/journal.pone.0232755
Rights: Attribution 4.0 International
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