Evidence map›Paper›PMID 23624404›Full record

ArticleNature cell biology2013

Role of Cdc48/p97 as a SUMO-targeted segregase curbing Rad51-Rad52 interaction.

Steven Bergink, Tim Ammon, Maximilian Kern, Lothar Schermelleh, Heinrich Leonhardt, Stefan Jentsch

Abstract read
PubMed Publisher
In one paragraph

Article in Nature cell biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 91 papers.

0numbers the graph read from it
0cells of the map it votes in
91citing papers in PubMed
7.5field-weighted citation impact, top 2% 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

91 citing papers in PubMed, 128 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Review
  8. Review
  9. Article
  10. Article
  11. SUMO enhances unfolding of SUMO-polyubiquitin-modified substrates by the Ufd1/Npl4/Cdc48 complex.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  12. SUMO control of centromere homeostasis.Frontiers in cell and developmental biology · 2023
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. USP7 and VCPCell reports · 2021
    Article
  18. Review
  19. Article
  20. Coordinating DNA Replication and Mitosis through Ubiquitin/SUMO and CDK1.International journal of molecular sciences · 2021
    Review

31 more citing papers are in PubMed but not listed here.

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

6 authors at 4 institutions in 1 country.

Steven BerginkDepartment of Molecular Cell Biology, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany.
Tim Ammon
Maximilian Kern
Lothar Schermelleh
Heinrich Leonhardt
Stefan Jentsch
Max Planck Institute of Biochemistry · DECenter for Integrated Protein Science Munich · DELudwig-Maximilians-Universität München · DEMax Planck Society · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cdc48 (also known as p97), a conserved chaperone-like ATPase, plays a strategic role in the ubiquitin system. Empowered by ATP-driven conformational changes, Cdc48 acts as a segregase by dislodging ubiquitylated proteins from their environment. Ufd1, a known co-factor of Cdc48, also binds SUMO (ref. 6), but whether SUMOylated proteins are subject to the segregase activity of Cdc48 as well and what these substrates are remains unknown. Here we show that Cdc48 with its co-factor Ufd1 is SUMO-targeted to proteins involved in DNA double-strand break repair. Cdc48 associates with SUMOylated Rad52, a factor that assembles the Rad51 recombinase on chromatin. By acting on the Rad52-Rad51 complex, Cdc48 curbs their physical interaction and displaces the proteins from DNA. Genetically interfering with SUMO-targeting or segregase activity leads to an increase in spontaneous recombination rates, accompanied by aberrant in vivo Rad51 foci formation in yeast and mammalian cells. Our data thus suggest that SUMO-targeted Cdc48 restricts the recombinase Rad51 by counterbalancing the activity of Rad52. We propose that Cdc48, through its ability to associate with co-factors that have affinities for ubiquitin and SUMO, connects the two modification pathways for protein degradation or other regulatory purposes.

Indexed as

DNA RepairAdenosine TriphosphatasesAnimalsBlotting, WesternCell Cycle ProteinsCell Line, TumorDNA Breaks, Double-StrandedDNA, FungalElectrophoresis, Polyacrylamide GelEnzyme ActivationHumansImmunoprecipitationMultiprotein ComplexesProtein BindingProtein Interaction MappingProteolysisAdenosine TriphosphatasesCDC48 protein, S cerevisiaeCell Cycle ProteinsDNA, FungalMultiprotein ComplexesRAD51 protein, S cerevisiaeRad51 RecombinaseRad52 DNA Repair and Recombination ProteinRAD52 protein, S cerevisiaeRecombinant ProteinsSaccharomyces cerevisiae ProteinsSmall Ubiquitin-Related Modifier ProteinsSMT3 protein, S cerevisiaeSUMO-1 ProteinSUMO1 protein, humanUbiquitin-Conjugating EnzymesUbiquitin-Conjugating Enzyme UBC9Valosin Containing Protein

Identifiers

PMID23624404
OpenAlexW2100929124

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.