Evidence map›Paper›PMID 15601997›Full record

ArticleNucleic acids research2004

Rad23 stabilizes Rad4 from degradation by the Ub/proteasome pathway.

Tatiana G Ortolan, Li Chen, Prasad Tongaonkar, Kiran Madura

Open access · bronzeAbstract read
In one paragraph

Article in Nucleic acids research, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
3.1field-weighted citation impact, top 8% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

The trial behind it

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.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

39 citing papers in PubMed, 87 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Divergent roles of Rad4 and Rad23 homologs inApplied and environmental microbiology · 2023
    Article
  5. Comparative Roles of Rad4A and Rad4B in Photoprotection ofJournal of fungi (Basel, Switzerland) · 2023
    Article
  6. Article
  7. Altitudinal Heterogeneity of UV Adaptation inJournal of fungi (Basel, Switzerland) · 2021
    Article
  8. Yeast Rpn4 Links the Proteasome and DNA Repair viaInternational journal of molecular sciences · 2020
    Article
  9. Article
  10. Article
  11. Architecture of the human XPC DNA repair and stem cell coactivator complex.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  12. Loss of RAD-23 Protects Against Models of Motor Neuron Disease by Enhancing Mutant Protein Clearance.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2015
    Article
  13. Review
  14. Article
  15. Review
  16. Functional and mechanistic studies of XPC DNA-repair complex as transcriptional coactivator in embryonic stem cells.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  17. Article
  18. Article
  19. Article
  20. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Tatiana G OrtolanDepartment of Biochemistry, Robert Wood Johnson Medical School, 683 Hoes Lane, Piscataway, NJ 08854, USA.
Li Chen
Prasad Tongaonkar
Kiran Madura
Johnson University · US

Funding

NCI NIH HHS CA-80835
6 · The paper itself

Abstract

Rad23 protein interacts with the nucleotide excision-repair (NER) factor Rad4, and the dimer can bind damaged DNA. Rad23 also binds ubiquitinated proteins and promotes their degradation by the proteasome. Rad23/proteasome interaction is required for efficient NER, although the specific role of the Ub/proteasome system in DNA repair is unclear. We report that the availability of Rad4 contributes significantly to the cellular tolerance to UV light. Mutations in the proteasome, and in genes encoding the ubiquitin-conjugating enzymes Ubc4 and Ubc5, stabilized Rad4 and increased tolerance to UV light. A short amino acid sequence, previously identified in human Rad23, mediates the interaction between Rad23 and Rad4. We determined that this motif was required for stabilizing Rad4, and could function independently of the intact protein. A ubiquitin-like (UbL) domain in Rad23 binds the proteasome, and is required for conferring full resistance to DNA damage. However, Rad23/proteasome interaction appears unrelated to Rad23-mediated stabilization of Rad4. Specifically, simultaneous expression of a Rad23 mutant that could not bind the proteasome, with a mutant that could not interact with Rad4, fully suppressed the UV sensitivity of rad23Delta, demonstrating that Rad23 performs two independent, but concurrent roles in NER.

Indexed as

DNA RepairAmino Acid SequenceBinding SitesDNA-Binding ProteinsMutationProteasome Endopeptidase ComplexProtein Structure, TertiarySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitin-Conjugating EnzymesUltraviolet RaysDNA-Binding ProteinsProteasome Endopeptidase ComplexRAD23 protein, S cerevisiaeRad4 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsUBC5 protein, S cerevisiaeUbiquitin-Conjugating Enzymesubiquitin-conjugating enzyme UBC4

Identifiers

PMID15601997
PMCPMC545455
OpenAlexW2105162444

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.