ArticleMolecular biology of the cell2010
Rad4 regulates protein turnover at a postubiquitylation step.
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 14 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
14 citing papers in PubMed, 19 citations in OpenAlex.
- Proteomic analysis of the S. cerevisiae response to the anticancer ruthenium complex KP1019.Metallomics : integrated biometal science · 2020Article
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- Comparative analysis of intracellular metabolites, proteins and their molecular functions in a flor yeast strain under two enological conditions.World journal of microbiology & biotechnology · 2018Article
- Article
- XPC: Going where no DNA damage sensor has gone before.DNA repair · 2015Review
- Glycosylation-directed quality control of protein folding.Nature reviews. Molecular cell biology · 2015Review
- Rad25 protein is targeted for degradation by the Ubc4-Ufd4 pathway.The Journal of biological chemistry · 2015Article
- Article
- Conserved miRNAs and their response to salt stress in wild eggplant Solanum linnaeanum roots.International journal of molecular sciences · 2014Article
- A Synthetic Interaction between CDC20 and RAD4 in Saccharomyces cerevisiae upon UV Irradiation.Molecular biology international · 2014Article
- XPC promotes MDM2-mediated degradation of the p53 tumor suppressor.Molecular biology of the cell · 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
- Oxidative stress and programmed cell death in yeast.Frontiers in oncology · 2012Article
- Rad7 E3 Ubiquitin Ligase Attenuates Polyubiquitylation of Rpn10 and Dsk2 Following DNA Damage inAdvances in biological chemistryArticle
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
The ubiquitin (Ub)-binding protein Rad23 plays an important role in facilitating the transfer of substrates to the proteasome. However, the mechanism underlying Rad23's function in proteolysis remains unknown. Here, we demonstrate that Rad4, a Rad23-binding protein, also regulates ubiquitylated substrate turnover. Rad4 was known previously only as a key repair factor that directly recognizes DNA damage and initiates DNA repair. Our results, however, reveal a novel function of Rad4. We found that Rad4 and Rad23 share several common substrates. Substrates in rad4Delta cells are ubiquitylated, indicating that Rad4 regulates a postubiquitylation event. Moreover, we found that Rad4 participates in the Rad23-Ufd2 pathway, but not the Rad23-Png1 pathway, consistent with previous findings that Png1 and Rad4 or Ufd2 form separate Rad23 complexes. The Rad4-binding domain is crucial for the functioning of Rad23 in degradation, suggesting that Rad4 and Rad23 work together in proteolysis. It is interesting to note that upon DNA damage, Rad4 becomes concentrated in the nucleus and degradation of the nonnuclear protein Pex29 is compromised, further suggesting that Rad4 may influence the coordination of various cellular processes. Our findings will help to unravel the detailed mechanisms underlying the roles of Rad23 and Rad4 in proteolysis and also the interplay between DNA repair and proteolysis.
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