The degradation-promoting roles of deubiquitinases Ubp6 and Ubp3 in cytosolic and ER protein quality control.
Journal
PloS one
ISSN: 1932-6203
Titre abrégé: PLoS One
Pays: United States
ID NLM: 101285081
Informations de publication
Date de publication:
2020
2020
Historique:
received:
06
02
2020
accepted:
21
04
2020
entrez:
14
5
2020
pubmed:
14
5
2020
medline:
30
7
2020
Statut:
epublish
Résumé
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.
Identifiants
pubmed: 32401766
doi: 10.1371/journal.pone.0232755
pii: PONE-D-20-03455
pmc: PMC7219781
doi:
Substances chimiques
Saccharomyces cerevisiae Proteins
0
Ubiquitin
0
Endopeptidases
EC 3.4.-
UBP3 protein, S cerevisiae
EC 3.4.99.-
UBP6 protein, S cerevisiae
EC 3.4.99.-
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
e0232755Déclaration de conflit d'intérêts
The authors have declared that no competing interests exist.
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