ArticleCurrent genetics2003
Investigating the importance of proteasome-interaction for Rad23 function.
Article in Current genetics, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
What it found
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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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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
13 citing papers in PubMed, 40 citations in OpenAlex.
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- Decoding ubiquitin for mitosis.Genes & cancer · 2012Article
- Ubiquitin-like and ubiquitin-associated domain proteins: significance in proteasomal degradation.Cellular and molecular life sciences : CMLS · 2009Review
- A novel connexin43-interacting protein, CIP75, which belongs to the UbL-UBA protein family, regulates the turnover of connexin43.The Journal of biological chemistry · 2008Article
- A conditional yeast E1 mutant blocks the ubiquitin-proteasome pathway and reveals a role for ubiquitin conjugates in targeting Rad23 to the proteasome.Molecular biology of the cell · 2007Article
- Yeast UBL-UBA proteins have partially redundant functions in cell cycle control.Cell division · 2006Article
- Scanning the human proteome for calmodulin-binding proteins.Proceedings of the National Academy of Sciences of the United States of America · 2005Article
- Structure of the XPC binding domain of hHR23A reveals hydrophobic patches for protein interaction.Protein science : a publication of the Protein Society · 2004Article
- The NEF4 complex regulates Rad4 levels and utilizes Snf2/Swi2-related ATPase activity for nucleotide excision repair.Molecular and cellular biology · 2004Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Rad23 contributes to diverse cellular functions that include DNA repair, stress response and growth control. An amino-terminal ubiquitin-like (UbL) domain in Rad23 interacts with catalytically active proteasomes and internal sequences bind multi-ubiquitinated proteins. Rad23 regulates the assembly of substrate-linked multi-ubiquitin chains, promotes efficient degradation of model substrates, and plays an overlapping role with the proteasome subunit, Rpn10. These and other results led to the hypothesis that Rad23 translocates proteolytic substrates to the proteasome to promote degradation. It was previously shown that the UbL domain in Rad23 could be functionally replaced by ubiquitin. However, monomeric ubiquitin does not bind the proteasome efficiently, and we therefore investigated whether proteasome interaction was required for all Rad23 functions. We report here that the ubiquitin moiety in Ub-rad23 is ubiquitinated in vivo and could provide an alternate mechanism for binding the proteasome. These results suggest that the localization of Rad23 to the proteasome, either by its UbL domain, or following ubiquitination of an amino-terminal ubiquitin moiety (Ub-rad23), is necessary for full activity.
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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.