Evidence map›Paper›PMID 16382133›Full record

ArticleMolecular and cellular biology2006

The transcriptional histone acetyltransferase cofactor TRRAP associates with the MRN repair complex and plays a role in DNA double-strand break repair.

Flavie Robert, Sara Hardy, Zita Nagy, Céline Baldeyron, Rabih Murr, Ugo Déry, Jean-Yves Masson, Dora Papadopoulo, Zdenko Herceg, Làszlò Tora

Abstract read
In one paragraph

Article in Molecular and cellular biology, 2006. 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
2.1field-weighted citation impact, top 13% 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, 76 citations in OpenAlex.

  1. Review
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  8. The histone variant H2A.Z in gene regulation.Epigenetics & chromatin · 2019
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  14. The role of ubiquitin-dependent segregase p97 (VCP or Cdc48) in chromatin dynamics after DNA double strand breaks.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2017
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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

10 authors at 4 institutions in 2 countries.

Flavie RobertDepartment of Transcription, Institut de Génétique et de Biologie Moleculaire et Cellulaire, UMR 7104 CNRS, F-67404 Illkirch Cedex, CU de Strasbourg, France.
Sara Hardy
Zita Nagy
Céline Baldeyron
Rabih Murr
Ugo Déry
Jean-Yves Masson
Dora Papadopoulo
Zdenko Herceg
Làszlò Tora
Institut de génétique et de biologie moléculaire et cellulaire · FRCentre International de Recherche sur le Cancer · FRHôtel-Dieu de Québec · CAInstitut Curie · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Transactivation-transformation domain-associated protein (TRRAP) is a component of several multiprotein histone acetyltransferase (HAT) complexes implicated in transcriptional regulation. TRRAP was shown to be required for the mitotic checkpoint and normal cell cycle progression. MRE11, RAD50, and NBS1 (product of the Nijmegan breakage syndrome gene) form the MRN complex that is involved in the detection, signaling, and repair of DNA double-strand breaks (DSBs). By using double immunopurification, mass spectrometry, and gel filtration, we describe the stable association of TRRAP with the MRN complex. The TRRAP-MRN complex is not associated with any detectable HAT activity, while the isolated other TRRAP complexes, containing either GCN5 or TIP60, are. TRRAP-depleted extracts show a reduced nonhomologous DNA end-joining activity in vitro. Importantly, small interfering RNA knockdown of TRRAP in HeLa cells or TRRAP knockout in mouse embryonic stem cells inhibit the DSB end-joining efficiency and the precise nonhomologous end-joining process, further suggesting a functional involvement of TRRAP in the DSB repair processes. Thus, TRRAP may function as a molecular link between DSB signaling, repair, and chromatin remodeling.

Indexed as

DNA DamageDNA RepairAcid Anhydride HydrolasesAdaptor Proteins, Signal TransducingAnimalsATP-Binding Cassette TransportersCell Cycle ProteinsCell Line, TumorChromatin Assembly and DisassemblyChromatography, GelDNA-Binding ProteinsDNA Repair EnzymesHistone AcetyltransferasesHumansLysine Acetyltransferase 5MiceAcid Anhydride HydrolasesAdaptor Proteins, Signal TransducingATP-Binding Cassette TransportersCell Cycle ProteinsDNA-Binding ProteinsDNA Repair EnzymesHistone AcetyltransferasesKAT5 protein, humanLysine Acetyltransferase 5Mre11a protein, mouseMRE11 Homologue ProteinMRE11 protein, humanNBN protein, humanNijmegen breakage syndrome 1 protein, mouseNuclear Proteinsp300-CBP-Associated Factorp300-CBP Transcription FactorsRAD50 protein, humanRad50 protein, mouseRNA, Small InterferingTranscription Factorstransformation-transcription domain-associated protein

Identifiers

PMID16382133
PMCPMC1346889
OpenAlexW2152385119

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

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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.