Evidence map›Paper›PMID 25817432›Full record

ArticleNature communications2015

Cmr1/WDR76 defines a nuclear genotoxic stress body linking genome integrity and protein quality control.

Irene Gallina, Camilla Colding, Peter Henriksen, Petra Beli, Kyosuke Nakamura, Judith Offman, David P Mathiasen, Sonia Silva, Eva Hoffmann, Anja Groth and 2 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed
4.8field-weighted citation impact, top 4% 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

55 citing papers in PubMed, 94 citations in OpenAlex.

  1. The role of the nucleus in the control of mitochondrial precursor proteins in yeast.Protein science : a publication of the Protein Society · 2026
    Review
  2. Article
  3. Article
  4. Article
  5. An integrated structural model of the DNA damage-responsive H3K4me3 binding WDR76:SPIN1 complex with the nucleosome.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  6. Article
  7. Article
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  10. Analysis of a Familial IgAN Accompanied by COL4A3 Mutation.Journal of inflammation research · 2024
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Quality control of cytoplasmic proteins inside the nucleus.Computational and structural biotechnology journal · 2022
    Review
  19. Review
  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

12 authors at 3 institutions in 2 countries.

Irene GallinaDepartment of Biology, University of Copenhagen, Room 4.1.07, Copenhagen N DK-2200, Denmark.
Camilla ColdingDepartment of Biology, University of Copenhagen, Room 4.1.07, Copenhagen N DK-2200, Denmark.
Peter HenriksenThe Novo Nordisk Foundation Center for Protein Research, Faculty of Health and Medical Sciences, University of Copenhagen, Copenhagen N DK-2200, Denmark.
Petra BeliThe Novo Nordisk Foundation Center for Protein Research, Faculty of Health and Medical Sciences, University of Copenhagen, Copenhagen N DK-2200, Denmark.
Kyosuke NakamuraBiotech Research and Innovation Centre (BRIC) and Centre for Epigenetics, University of Copenhagen, Copenhagen N DK-2200, Denmark.
Judith OffmanMRC, Centre for Genome Damage and Stability, School of Life Sciences, University of Sussex, Brighton BN1 9RH, UK.
David P MathiasenDepartment of Biology, University of Copenhagen, Room 4.1.07, Copenhagen N DK-2200, Denmark.
Sonia SilvaDepartment of Biology, University of Copenhagen, Room 4.1.07, Copenhagen N DK-2200, Denmark.
Eva HoffmannMRC, Centre for Genome Damage and Stability, School of Life Sciences, University of Sussex, Brighton BN1 9RH, UK.
Anja GrothBiotech Research and Innovation Centre (BRIC) and Centre for Epigenetics, University of Copenhagen, Copenhagen N DK-2200, Denmark.
Chunaram ChoudharyThe Novo Nordisk Foundation Center for Protein Research, Faculty of Health and Medical Sciences, University of Copenhagen, Copenhagen N DK-2200, Denmark.
Michael LisbyDepartment of Biology, University of Copenhagen, Room 4.1.07, Copenhagen N DK-2200, Denmark.
University of Copenhagen · DKNovo Nordisk Foundation · DKUniversity of Sussex · GB

Funding

Cancer Research UKEuropean Research Council 242905European Research Council 281765Medical Research Council
6 · The paper itself

Abstract

DNA replication stress is a source of genomic instability. Here we identify changed mutation rate 1 (Cmr1) as a factor involved in the response to DNA replication stress in Saccharomyces cerevisiae and show that Cmr1--together with Mrc1/Claspin, Pph3, the chaperonin containing TCP1 (CCT) and 25 other proteins--define a novel intranuclear quality control compartment (INQ) that sequesters misfolded, ubiquitylated and sumoylated proteins in response to genotoxic stress. The diversity of proteins that localize to INQ indicates that other biological processes such as cell cycle progression, chromatin and mitotic spindle organization may also be regulated through INQ. Similar to Cmr1, its human orthologue WDR76 responds to proteasome inhibition and DNA damage by relocalizing to nuclear foci and physically associating with CCT, suggesting an evolutionarily conserved biological function. We propose that Cmr1/WDR76 plays a role in the recovery from genotoxic stress through regulation of the turnover of sumoylated and phosphorylated proteins.

Indexed as

Genomic InstabilityAmino Acid Transport SystemsCell Cycle CheckpointsCell Cycle ProteinsChaperonin Containing TCP-1ChromatinChromosomal Proteins, Non-HistoneDNA-Binding ProteinsDNA DamageHeat-Shock ProteinsHeat-Shock Proteins, SmallHeLa CellsHumansMutationPhosphoprotein PhosphatasesProteasome Endopeptidase ComplexAmino Acid Transport SystemsBTN2 protein, S cerevisiaeCell Cycle ProteinsChaperonin Containing TCP-1ChromatinChromosomal Proteins, Non-HistoneCmr1 protein, S cerevisiaeCTF18 protein, S cerevisiaeDNA-Binding ProteinsHeat-Shock ProteinsHeat-Shock Proteins, SmallHSP42 protein, S cerevisiaeMRC1 protein, S cerevisiaePhosphoprotein PhosphatasesPPH3 protein, S cerevisiaeProteasome Endopeptidase ComplexProteinsSaccharomyces cerevisiae ProteinsVesicular Transport ProteinsWDR76 protein, human

Identifiers

PMID25817432
PMCPMC4389229
OpenAlexW2032390685

What OpenQuestion holds

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LicenceCC BY
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.