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The Roles of the Ubiquitin-Proteasome System in the Endoplasmic Reticulum Stress Pathway

Overview
Journal Int J Mol Sci
Publisher MDPI
Date 2021 Feb 6
PMID 33546413
Citations 38
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Abstract

The endoplasmic reticulum (ER) is a highly dynamic organelle in eukaryotic cells, which is essential for synthesis, processing, sorting of protein and lipid metabolism. However, the cells activate a defense mechanism called endoplasmic reticulum stress (ER stress) response and initiate unfolded protein response (UPR) as the unfolded proteins exceed the folding capacity of the ER due to the environmental influences or increased protein synthesis. ER stress can mediate many cellular processes, including autophagy, apoptosis and senescence. The ubiquitin-proteasome system (UPS) is involved in the degradation of more than 80% of proteins in the cells. Today, increasing numbers of studies have shown that the two important components of UPS, E3 ubiquitin ligases and deubiquitinases (DUBs), are tightly related to ER stress. In this review, we summarized the regulation of the E3 ubiquitin ligases and DUBs in ER stress.

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References
1.
Kwasna D, Abdul Rehman S, Natarajan J, Matthews S, Madden R, De Cesare V . Discovery and Characterization of ZUFSP/ZUP1, a Distinct Deubiquitinase Class Important for Genome Stability. Mol Cell. 2018; 70(1):150-164.e6. PMC: 5896202. DOI: 10.1016/j.molcel.2018.02.023. View

2.
Rong J, Chen L, Toth J, Tcherpakov M, Petroski M, Reed J . Bifunctional apoptosis regulator (BAR), an endoplasmic reticulum (ER)-associated E3 ubiquitin ligase, modulates BI-1 protein stability and function in ER Stress. J Biol Chem. 2010; 286(2):1453-63. PMC: 3020754. DOI: 10.1074/jbc.M110.175232. View

3.
Ozcan U, Cao Q, Yilmaz E, Lee A, Iwakoshi N, Ozdelen E . Endoplasmic reticulum stress links obesity, insulin action, and type 2 diabetes. Science. 2004; 306(5695):457-61. DOI: 10.1126/science.1103160. View

4.
Almanza A, Carlesso A, Chintha C, Creedican S, Doultsinos D, Leuzzi B . Endoplasmic reticulum stress signalling - from basic mechanisms to clinical applications. FEBS J. 2018; 286(2):241-278. PMC: 7379631. DOI: 10.1111/febs.14608. View

5.
Gu H, Li Q, Huang S, Lu W, Cheng F, Gao P . Mitochondrial E3 ligase March5 maintains stemness of mouse ES cells via suppression of ERK signalling. Nat Commun. 2015; 6:7112. PMC: 4458872. DOI: 10.1038/ncomms8112. View