Evidence map›Paper›PMID 26095369›Full record

ArticleNature communications2015

TRIM29 regulates the assembly of DNA repair proteins into damaged chromatin.

Yasushi Masuda, Hidehisa Takahashi, Shigeo Sato, Chieri Tomomori-Sato, Anita Saraf, Michael P Washburn, Laurence Florens, Ronald C Conaway, Joan W Conaway, Shigetsugu Hatakeyama

Open access · goldAbstract read
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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 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

45 citing papers in PubMed, 66 citations in OpenAlex.

  1. Review
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  14. When DNA-damage responses meet innate and adaptive immunity.Cellular and molecular life sciences : CMLS · 2024
    Review
  15. Article
  16. Article
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  19. TRIM56 promotes malignant progression of glioblastoma by stabilizing cIAP1 protein.Journal of experimental & clinical cancer research : CR · 2022
    Article
  20. Article
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 3 institutions in 2 countries.

Yasushi MasudaDepartment of Biochemistry, Hokkaido University Graduate School of Medicine, Kita 15, Nishi 7, Kita-ku, Sapporo, Hokkaido 060-8638, Japan.
Hidehisa TakahashiDepartment of Biochemistry, Hokkaido University Graduate School of Medicine, Kita 15, Nishi 7, Kita-ku, Sapporo, Hokkaido 060-8638, Japan.
Shigeo SatoStowers Institute for Medical Research, 1000 East, 50th Street, Kansas City, Missouri 64110, USA.
Chieri Tomomori-SatoStowers Institute for Medical Research, 1000 East, 50th Street, Kansas City, Missouri 64110, USA.
Anita SarafStowers Institute for Medical Research, 1000 East, 50th Street, Kansas City, Missouri 64110, USA.
Michael P WashburnStowers Institute for Medical Research, 1000 East, 50th Street, Kansas City, Missouri 64110, USA.
Laurence FlorensStowers Institute for Medical Research, 1000 East, 50th Street, Kansas City, Missouri 64110, USA.
Ronald C ConawayStowers Institute for Medical Research, 1000 East, 50th Street, Kansas City, Missouri 64110, USA.
Joan W ConawayStowers Institute for Medical Research, 1000 East, 50th Street, Kansas City, Missouri 64110, USA.
Shigetsugu HatakeyamaDepartment of Biochemistry, Hokkaido University Graduate School of Medicine, Kita 15, Nishi 7, Kita-ku, Sapporo, Hokkaido 060-8638, Japan.
Stowers Institute for Medical Research · USHokkaido University · JPUniversity Medical Center · US

Funding

BIOCHEMISTRY OF EUKARYOTIC MESSENGER RNA SYNTHESISR37GM041628 · NIGMS · STOWERS INSTITUTE FOR MEDICAL RESEARCH · PI CONAWAY, RONALD C. · 2000 to 2009
$3.8M
BIOCHEMISTRY OF EUKARYOTIC MESSENGER SYNTHESISR01GM041628 · NIGMS · UNIVERSITY OF TEXAS AUSTIN · PI CONAWAY, JOAN W, CONAWAY, RONALD C. · 1989 to 2013
$1.5M
NIGMS NIH HHS GM41628NIGMS NIH HHS R01 GM041628
6 · The paper itself

Abstract

Although DNA double-strand break (DSB) repair is mediated by numerous proteins accumulated at DSB sites, how DNA repair proteins are assembled into damaged chromatin has not been fully elucidated. Here we show that a member of the tripartite motif protein family, TRIM29, is a histone-binding protein responsible for DNA damage response (DDR). We found that TRIM29 interacts with BRCA1-associated surveillance complex, cohesion, DNA-PKcs and components of TIP60 complex. The dynamics of the TRIM29-containing complex on H2AX nucleosomes is coordinated by a cross-talk between histone modifications. TRIM29 binds to modified histone H3 and H4 tails in the context of nucleosomes. Furthermore, chromatin binding of TRIM29 is required for the phosphorylation of H2AX and cell viability in response to ionizing radiation. Our results suggest that TRIM29 functions as a scaffold protein to assemble DNA repair proteins into chromatin followed by efficient activation of DDR.

Indexed as

DNA DamageCell SurvivalChromatinDNA-Binding ProteinsDNA Repair EnzymesHEK293 CellsHeLa CellsHistone AcetyltransferasesHistonesHomeodomain ProteinsHumansImmunoprecipitationIn Vitro TechniquesLysine Acetyltransferase 5Mass SpectrometryMutS Homolog 2 ProteinBRAP protein, humanChromatinDMAP1 protein, humanDNA-Binding ProteinsDNA Repair EnzymesH2AX protein, humanHistone AcetyltransferasesHistonesHomeodomain ProteinsING3 protein, humanKAT5 protein, humanLysine Acetyltransferase 5MSH2 protein, humanMutS Homolog 2 ProteinNucleosomesRepressor ProteinsTranscription FactorsTRIM29 protein, humanTumor Suppressor ProteinsUbiquitin-Protein Ligases

Identifiers

PMID26095369
OpenAlexW1668815300

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.