ArticleThe Journal of biological chemistry2010
Yeast deubiquitinase Ubp3 interacts with the 26 S proteasome to facilitate Rad4 degradation.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
22 citing papers in PubMed, 32 citations in OpenAlex.
- When the chains do not break: the role of USP10 in physiology and pathology.Cell death & disease · 2020Review
- Formation and Recognition of UV-Induced DNA Damage within Genome Complexity.International journal of molecular sciences · 2020Review
- Releasing the Lockdown: An Emerging Role for the Ubiquitin-Proteasome System in the Breakdown of Transient Protein Inclusions.Biomolecules · 2020Review
- Lsm12 Mediates Deubiquitination of DNA Polymerase η To HelpApplied and environmental microbiology · 2019Article
- Single-nucleotide resolution dynamic repair maps of UV damage inProceedings of the National Academy of Sciences of the United States of America · 2018Article
- Proteasome storage granules protect proteasomes from autophagic degradation upon carbon starvation.eLife · 2018Article
- The exocyst subunit Sec3 is regulated by a protein quality control pathway.The Journal of biological chemistry · 2017Article
- The pleiotropic deubiquitinase Ubp3 confers aneuploidy tolerance.Genes & development · 2016Article
- XPC: Going where no DNA damage sensor has gone before.DNA repair · 2015Review
- Both the autophagy and proteasomal pathways facilitate the Ubp3p-dependent depletion of a subset of translation and RNA turnover factors during nitrogen starvation in Saccharomyces cerevisiae.RNA (New York, N.Y.) · 2015Article
- Identifying USPs regulating immune signals in Drosophila: USP2 deubiquitinates Imd and promotes its degradation by interacting with the proteasome.Cell communication and signaling : CCS · 2014Article
- Protein quality control in the nucleus.Biomolecules · 2014Review
- Loss of Ubp3 increases silencing, decreases unequal recombination in rDNA, and shortens the replicative life span in Saccharomyces cerevisiae.Molecular biology of the cell · 2014Article
- Opposing roles of Ubp3-dependent deubiquitination regulate replicative life span and heat resistance.The EMBO journal · 2014Article
- A chaperone-assisted degradation pathway targets kinetochore proteins to ensure genome stability.PLoS genetics · 2014Article
- Detection of an altered heterochromatin structure in the absence of the nucleotide excision repair protein Rad4 in Saccharomyces cerevisiae.Cell cycle (Georgetown, Tex.) · 2013Article
- Dynamic ubiquitination of the mitogen-activated protein kinase kinase (MAPKK) Ste7 determines mitogen-activated protein kinase (MAPK) specificity.The Journal of biological chemistry · 2013Article
- Loss of a 20S proteasome activator in Saccharomyces cerevisiae downregulates genes important for genomic integrity, increases DNA damage, and selectively sensitizes cells to agents with diverse mechanisms of action.G3 (Bethesda, Md.) · 2012Article
- Oxidative stress and programmed cell death in yeast.Frontiers in oncology · 2012Article
- A role for SUMO in nucleotide excision repair.DNA repair · 2011Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Deubiquitinating enzymes (DUBs) function in a variety of cellular processes by removing ubiquitin moieties from substrates, but their role in DNA repair has not been elucidated. Yeast Rad4-Rad23 heterodimer is responsible for recognizing DNA damage in nucleotide excision repair (NER). Rad4 binds to UV damage directly while Rad23 stabilizes Rad4 from proteasomal degradation. Here, we show that disruption of yeast deubiquitinase UBP3 leads to enhanced UV resistance, increased repair of UV damage and Rad4 levels in rad23Δ cells, and elevated Rad4 stability. A catalytically inactive Ubp3 (Ubp3-C469A), however, is unable to affect NER or Rad4. Consistent with its role in down-regulating Rad4, Ubp3 physically interacts with Rad4 and the proteasome, both in vivo and in vitro, suggesting that Ubp3 associates with the proteasome to facilitate Rad4 degradation and thus suppresses NER.
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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.