ArticleMolecular biology of the cell2010
A nucleus-based quality control mechanism for cytosolic proteins.
Article in Molecular biology of the cell, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 90 papers.
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Who cites it
90 citing papers in PubMed.
- The role of the nucleus in the control of mitochondrial precursor proteins in yeast.Protein science : a publication of the Protein Society · 2026Review
- Article
- Quiescent cells maintain active degradation-mediated protein quality control requiring proteasome, autophagy, and nucleus-vacuole junctions.The Journal of biological chemistry · 2025Article
- Degradation of citrate synthase lacking the mitochondrial targeting sequence is inhibited in cells defective in Hsp70/Hsp40 chaperones under heat stress conditions.FEMS yeast research · 2024Article
- UPL5 modulates WHY2 protein distribution in a Kub-site dependent ubiquitination in response to [CaiScience · 2023Article
- Phase separation and pathologic transitions of RNP condensates in neurons: implications for amyotrophic lateral sclerosis, frontotemporal dementia and other neurodegenerative disorders.Frontiers in molecular neuroscience · 2023Review
- The role of ubiquitination in spinal and bulbar muscular atrophy.Frontiers in molecular neuroscience · 2022Review
- Quality control of cytoplasmic proteins inside the nucleus.Computational and structural biotechnology journal · 2022Review
- Ubiquitin Ligase Redundancy and Nuclear-Cytoplasmic Localization in Yeast Protein Quality Control.Biomolecules · 2021Review
- Distinct classes of misfolded proteins differentially affect the growth of yeast compromised for proteasome function.FEBS letters · 2021Article
- Nuclear envelope budding is a response to cellular stress.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Article
- Protein quality control degron-containing substrates are differentially targeted in the cytoplasm and nucleus by ubiquitin ligases.Genetics · 2021Article
- UBE2S interacting with TRIM28 in the nucleus accelerates cell cycle by ubiquitination of p27 to promote hepatocellular carcinoma development.Signal transduction and targeted therapy · 2021Article
- Nuclear Ubiquitin-Proteasome Pathways in Proteostasis Maintenance.Biomolecules · 2021Review
- Differential role of cytosolic Hsp70s in longevity assurance and protein quality control.PLoS genetics · 2021Article
- Direct involvement of Hsp70 ATP hydrolysis in Ubr1-dependent quality control.Molecular biology of the cell · 2020Article
- The yeastJournal of cell science · 2020Article
- Chaperone-Mediated Protein Disaggregation Triggers Proteolytic Clearance of Intra-nuclear Protein Inclusions.Cell reports · 2020Article
- Genetic Selection Based on a Ste6G3 (Bethesda, Md.) · 2020Article
30 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Intracellular quality control systems monitor protein conformational states. Irreversibly misfolded proteins are cleared through specialized degradation pathways. Their importance is underscored by numerous pathologies caused by aberrant proteins. In the cytosol, where most proteins are synthesized, quality control remains poorly understood. Stress-inducible chaperones and the 26S proteasome are known mediators but how their activities are linked is unclear. To better understand these mechanisms, a panel of model misfolded substrates was analyzed in detail. Surprisingly, their degradation occurs not in the cytosol but in the nucleus. Degradation is dependent on the E3 ubiquitin ligase San1p, known previously to direct the turnover of damaged nuclear proteins. A second E3 enzyme, Ubr1p, augments this activity but is insufficient by itself. San1p and Ubr1p are not required for nuclear import of substrates. Instead, the Hsp70 chaperone system is needed for efficient import and degradation. These data reveal a new function of the nucleus as a compartment central to the quality control of cytosolic proteins.
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Registered trials
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