Evidence map›Paper›PMID 25183520›Full record

ArticleNucleic acids research2014

The ubiquitin-selective chaperone Cdc48/p97 associates with Ubx3 to modulate monoubiquitylation of histone H2B.

Mélanie Bonizec, Lucas Hérissant, Wojciech Pokrzywa, Fuqiang Geng, Sabine Wenzel, Gregory C Howard, Paco Rodriguez, Sabine Krause, William P Tansey, Thorsten Hoppe and 1 more

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.1field-weighted citation impact, top 22% 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

11 citing papers in PubMed, 16 citations in OpenAlex.

  1. Review
  2. Article
  3. iScience · 2023
    Article
  4. bioRxiv : the preprint server for biology · 2023
    Article
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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

11 authors at 6 institutions in 3 countries.

Mélanie BonizecSorbonne Paris Cité, INSERM UMR944, CNRS UMR7212, Equipe labellisée Ligue contre le cancer, University of Paris Diderot, Hôpital St. Louis 1, Avenue Claude Vellefaux 75475 Paris Cedex 10, France.
Lucas HérissantSorbonne Paris Cité, INSERM UMR944, CNRS UMR7212, Equipe labellisée Ligue contre le cancer, University of Paris Diderot, Hôpital St. Louis 1, Avenue Claude Vellefaux 75475 Paris Cedex 10, France.
Wojciech PokrzywaInstitute for Genetics and Cologne Excellence Cluster on Cellular Stress Responses in Aging-Associated Diseases (CECAD), University of Cologne, Joseph-Stelzmann-Str. 26, 50931 Cologne, Germany.
Fuqiang GengDepartment of Cell and Developmental Biology, Vanderbilt University School of Medicine, 465 21st Avenue South, Nashville, TN 37232, USA.
Sabine WenzelDepartment of Cell and Developmental Biology, Vanderbilt University School of Medicine, 465 21st Avenue South, Nashville, TN 37232, USA.
Gregory C HowardDepartment of Cell and Developmental Biology, Vanderbilt University School of Medicine, 465 21st Avenue South, Nashville, TN 37232, USA.
Paco RodriguezSorbonne Paris Cité, INSERM UMR944, CNRS UMR7212, Equipe labellisée Ligue contre le cancer, University of Paris Diderot, Hôpital St. Louis 1, Avenue Claude Vellefaux 75475 Paris Cedex 10, France.
Sabine KrauseLaboratory for Molecular Myology, Friedrich Baur Institute, Department of Neurology, Ludwig Maximilians University, Munich, Germany.
William P TanseyDepartment of Cell and Developmental Biology, Vanderbilt University School of Medicine, 465 21st Avenue South, Nashville, TN 37232, USA.
Thorsten HoppeInstitute for Genetics and Cologne Excellence Cluster on Cellular Stress Responses in Aging-Associated Diseases (CECAD), University of Cologne, Joseph-Stelzmann-Str. 26, 50931 Cologne, Germany.
Catherine DargemontSorbonne Paris Cité, INSERM UMR944, CNRS UMR7212, Equipe labellisée Ligue contre le cancer, University of Paris Diderot, Hôpital St. Louis 1, Avenue Claude Vellefaux 75475 Paris Cedex 10, France catherine.dargemont@inserm.fr.
Vanderbilt University · USInserm · FRCentre National de la Recherche Scientifique · FRCologne Excellence Cluster on Cellular Stress Responses in Aging Associated Diseases · DELudwig-Maximilians-Universität München · DEUniversity of Cologne · DE

Funding

Tumor Immunology and Microenvironment Research ProgramP30CA068485 · NCI · VANDERBILT UNIVERSITY MEDICAL CENTER · PI MATTHEW J TYSKA · 1995 to 2026
$172.8M
Transcription Control By The Ubiquitin-Proteasome SystemR01GM067728 · NIGMS · VANDERBILT UNIVERSITY · PI TANSEY, WILLIAM PATRICK · 2003 to 2015
$4.6M
NCI NIH HHS P30CA68485NIGMS NIH HHS GM067728NIGMS NIH HHS R01 GM067728
6 · The paper itself

Abstract

Cdc48/p97 is an evolutionary conserved ubiquitin-dependent chaperone involved in a broad array of cellular functions due to its ability to associate with multiple cofactors. Aside from its role in removing RNA polymerase II from chromatin after DNA damage, little is known about how this AAA-ATPase is involved in the transcriptional process. Here, we show that yeast Cdc48 is recruited to chromatin in a transcription-coupled manner and modulates gene expression. Cdc48, together with its cofactor Ubx3 controls monoubiquitylation of histone H2B, a conserved modification regulating nucleosome dynamics and chromatin organization. Mechanistically, Cdc48 facilitates the recruitment of Lge1, a cofactor of the H2B ubiquitin ligase Bre1. The function of Cdc48 in controlling H2B ubiquitylation appears conserved in human cells because disease-related mutations or chemical inhibition of p97 function affected the amount of ubiquitylated H2B in muscle cells. Together, these results suggest a prominent role of Cdc48/p97 in the coordination of chromatin remodeling with gene transcription to define cellular differentiation processes.

Indexed as

Transcription, GeneticUbiquitinationAdenosine TriphosphatasesCell Cycle ProteinsCell LineCells, CulturedFemaleHistonesHumansMaleMolecular ChaperonesMutationMyoblastsSaccharomyces cerevisiae ProteinsTranscription FactorsValosin Containing ProteinAdenosine TriphosphatasesCDC48 protein, S cerevisiaeCell Cycle ProteinsHistonesLge1 protein, S cerevisiaeMolecular ChaperonesSaccharomyces cerevisiae ProteinsTranscription FactorsUbx3 protein, S cerevisiaeValosin Containing Protein

Identifiers

PMID25183520
PMCPMC4176170
OpenAlexW2167836418

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.