ArticleThe Journal of biological chemistry2011
Nuclear protein quality is regulated by the ubiquitin-proteasome system through the activity of Ubc4 and San1 in fission yeast.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed.
- The ortholog of human DNAJC9 promotes histone H3-H4 degradation and is counteracted by Asf1 in fission yeast.Nucleic acids research · 2025Article
- Article
- Comparative Genomics Reveals a Single Nucleotide Deletion inFrontiers in fungal biology · 2022Article
- The San1 Ubiquitin Ligase Avidly Recognizes Misfolded Proteins through Multiple Substrate Binding Sites.Biomolecules · 2021Article
- Protein quality control in the nucleus.Current opinion in cell biology · 2016Review
- A conserved RAD6-MDM2 ubiquitin ligase machinery targets histone chaperone ASF1A in tumorigenesis.Oncotarget · 2015Article
- Protein quality control in the nucleus.Biomolecules · 2014Review
- How the nucleus copes with proteotoxic stress.Current biology : CB · 2014Review
- Cellular maintenance of nuclear protein homeostasis.Cellular and molecular life sciences : CMLS · 2014Review
- A chaperone-assisted degradation pathway targets kinetochore proteins to ensure genome stability.PLoS genetics · 2014Article
- E3 ubiquitin ligase Pub1 is implicated in endocytosis of a GPI-anchored protein Ecm33 in fission yeast.PloS one · 2014Article
- Human cytomegalovirus UL76 elicits novel aggresome formation via interaction with S5a of the ubiquitin proteasome system.Journal of virology · 2013Article
- Means of self-preservation: how an intrinsically disordered ubiquitin-protein ligase averts self-destruction.Molecular biology of the cell · 2013Article
- Misfolded proteins recognition strategies of E3 ubiquitin ligases and neurodegenerative diseases.Molecular neurobiology · 2013Review
- Selective destruction of abnormal proteins by ubiquitin-mediated protein quality control degradation.Seminars in cell & developmental biology · 2012Review
- The yeast ubr1 ubiquitin ligase participates in a prominent pathway that targets cytosolic thermosensitive mutants for degradation.G3 (Bethesda, Md.) · 2012Article
- Nucleocytoplasmic shuttling of cytoskeletal proteins: molecular mechanism and biological significance.International journal of cell biology · 2012Article
- Histone chaperone Asf1 plays an essential role in maintaining genomic stability in fission yeast.PloS one · 2012Article
- Multistep regulation of protein kinase A in its localization, phosphorylation and binding with a regulatory subunit in fission yeast.Current genetics · 2011Article
- Exposed hydrophobicity is a key determinant of nuclear quality control degradation.Molecular biology of the cell · 2011Article
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6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Eukaryotic cells monitor and maintain protein quality through a set of protein quality control (PQC) systems whose role is to minimize the harmful effects of the accumulation of aberrant proteins. Although these PQC systems have been extensively studied in the cytoplasm, nuclear PQC systems are not well understood. The present work shows the existence of a nuclear PQC system mediated by the ubiquitin-proteasome system in the fission yeast Schizosaccharomyces pombe. Asf1-30, a mutant form of the histone chaperone Asf1, was used as a model substrate for the study of the nuclear PQC. A temperature-sensitive Asf1-30 protein localized to the nucleus was selectively degraded by the ubiquitin-proteasome system. The Asf1-30 mutant protein was highly ubiquitinated at higher temperatures, and it remained stable in an mts2-1 mutant, which lacks proteasome activity. The E2 enzyme Ubc4 was identified among 11 candidate proteins as the ubiquitin-conjugating enzyme in this system, and San1 was selected among 100 candidates as the ubiquitin ligase (E3) targeting Asf1-30 for degradation. San1, but not other nuclear E3s, showed specificity for the mutant nuclear Asf1-30, but did not show activity against wild-type Asf1. These data clearly showed that the aberrant nuclear protein was degraded by a defined set of E1-E2-E3 enzymes through the ubiquitin-proteasome system. The data also show, for the first time, the presence of a nuclear PQC system in fission yeast.
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