ArticleNature communications2016
Deubiquitinase activity is required for the proteasomal degradation of misfolded cytosolic proteins upon heat-stress.
Article in Nature communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 67 citations in OpenAlex.
- Evolutionary tuning of the molecular charge state of UBP24 shapes responses to high temperature.Nature plants · 2026Article
- CIRCADIAN CLOCK-ASSOCIATED 1 represses thermotolerance by inhibitingHorticulture research · 2026Article
- Endothelial KSR2 regulated by genetic variation protects against atherosclerosis through AMPKα1 stabilization.Theranostics · 2026Article
- The Ubiquitin Script: writing protein fates in chains.Essays in biochemistry · 2025Review
- Crucial roles of Grr1 in splicing and translation of HAC1 mRNA upon unfolded stress response.Nature communications · 2025Article
- Light-Activatable Ubiquitin for Studying Linkage-Specific Ubiquitin Chain Formation Kinetics.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Stalled disomes marked by Hel2-dependent ubiquitin chains undergo Ubp2/Ubp3-mediated deubiquitination upon translational run-off.Communications biology · 2025Article
- Responses of the tree peony (Paeonia suffruticosa, Paeoniaceae) cultivar 'Yu Hong' to heat stress revealed by iTRAQ-based quantitative proteomics.Proteome science · 2022Article
- USP5 enhances SGTA mediated protein quality control.PloS one · 2022Article
- Deubiquitinating enzymes (DUBs): Regulation, homeostasis, and oxidative stress response.The Journal of biological chemistry · 2021Review
- Ubiquitination is essential for recovery of cellular activities after heat shock.Science (New York, N.Y.) · 2021Article
- It's not just a phase; ubiquitination in cytosolic protein quality control.Biochemical Society transactions · 2021Review
- Emerging functions of branched ubiquitin chains.Cell discovery · 2021Review
- Deubiquitylating enzymes in neuronal health and disease.Cell death & disease · 2021Review
- Proteomics-Based Identification of DUB Substrates Using Selective Inhibitors.Cell chemical biology · 2021Article
- The structure and function of deubiquitinases: lessons from budding yeast.Open biology · 2020Review
- Precise Replacement ofG3 (Bethesda, Md.) · 2020Article
- Autophagy is a pro-survival adaptive response to heat shock in bovine cumulus-oocyte complexes.Scientific reports · 2020Article
- Co-Chaperones in Targeting and Delivery of Misfolded Proteins to the 26S Proteasome.Biomolecules · 2020Review
- Genetic Selection Based on a Ste6G3 (Bethesda, Md.) · 2020Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
Elimination of misfolded proteins is crucial for proteostasis and to prevent proteinopathies. Nedd4/Rsp5 emerged as a major E3-ligase involved in multiple quality control pathways that target misfolded plasma membrane proteins, aggregated polypeptides and cytosolic heat-induced misfolded proteins for degradation. It remained unclear how in one case cytosolic heat-induced Rsp5 substrates are destined for proteasomal degradation, whereas other Rsp5 quality control substrates are otherwise directed to lysosomal degradation. Here we find that Ubp2 and Ubp3 deubiquitinases are required for the proteasomal degradation of cytosolic misfolded proteins targeted by Rsp5 after heat-shock (HS). The two deubiquitinases associate more with Rsp5 upon heat-stress to prevent the assembly of K63-linked ubiquitin on Rsp5 heat-induced substrates. This activity was required to promote the K48-mediated proteasomal degradation of Rsp5 HS-induced substrates. Our results indicate that ubiquitin chain editing is key to the cytosolic protein quality control under stress conditions.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.