Evidence map›Paper›PMID 26976643›Full record

ArticleMolecular and cellular biology2016

Coordinated Regulation of TIP60 and Poly(ADP-Ribose) Polymerase 1 in Damaged-Chromatin Dynamics.

Masae Ikura, Kanji Furuya, Atsuhiko Fukuto, Ryo Matsuda, Jun Adachi, Tomonari Matsuda, Akira Kakizuka, Tsuyoshi Ikura

Open access · bronzeAbstract read
In one paragraph

Article in Molecular and cellular biology, 2016. 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
0.9field-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, 22 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
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  6. Impact of NuclearMolecular and cellular biology · 2022
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  7. Review
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  9. RANBP9 as potential therapeutic target in non-small cell lung cancer.Journal of cancer metastasis and treatment · 2020
    Article
  10. Review
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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

8 authors at 3 institutions in 1 country.

Masae IkuraLaboratory of Chromatin Regulatory Network, Department of Mutagenesis, Radiation Biology Center, Kyoto University, Kyoto, Japan.
Kanji FuruyaDepartment of Radiation Systems, Radiation Biology Center, Kyoto University, Kyoto, Japan.
Atsuhiko FukutoDepartment of Ophthalmology and Visual Science, Graduate School of Biomedical Sciences, Hiroshima University, Hiroshima, Japan.
Ryo MatsudaLaboratory of Chromatin Regulatory Network, Department of Mutagenesis, Radiation Biology Center, Kyoto University, Kyoto, Japan.
Jun AdachiNational Institute of Biomedical Innovation, Ibaraki, Osaka, Japan.
Tomonari MatsudaLaboratory of Environment Quality Management, Research Center for Environmental Quality Management, Kyoto University, Shiga, Japan.
Akira KakizukaLaboratory of Functional Biology, Kyoto University Graduate School of Biostudies, Kyoto, Japan.
Tsuyoshi IkuraLaboratory of Chromatin Regulatory Network, Department of Mutagenesis, Radiation Biology Center, Kyoto University, Kyoto, Japan ikurat@house.rbc.kyoto-u.ac.jp.
Kyoto University · JPHiroshima University · JPNational Institute of Biomedical Innovation, Health and Nutrition · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The dynamic exchange of histones alleviates the nucleosome barrier and simultaneously facilitates various aspects of cellular DNA metabolism, such as DNA repair and transcription. In response to DNA damage, the acetylation of Lys5 in the histone variant H2AX, catalyzed by TIP60, plays a key role in promoting histone exchange; however, the detailed molecular mechanism still is unclear. Here, we show that the TIP60 complex includes poly(ADP-ribose) polymerase 1 (PARP-1). PARP-1 is required for the rapid exchange of H2AX on chromatin at DNA damage sites. It is known that PARP-1 binds dynamically to damaged chromatin and is crucial for the subsequent recruitment of other repair factors, and its auto-poly(ADP-ribosyl)ation is required for the dynamics. We also show that the acetylation of histone H2AX at Lys5 by TIP60, but not the phosphorylation of H2AX, is required for the ADP-ribosylation activity of PARP-1 and its dynamic binding to damaged chromatin. Our results indicate the reciprocal regulation of K5 acetylation of H2AX and PARP-1, which could modulate the chromatin structure to facilitate DNA metabolism at damage sites. This could explain the rather undefined roles of PARP-1 in various DNA damage responses.

Indexed as

Chromatin Assembly and DisassemblyAcetylationAnimalsDNA DamageHeLa CellsHistone AcetyltransferasesHistonesHumansLysineLysine Acetyltransferase 5MicePhosphorylationPoly (ADP-Ribose) Polymerase-1H2AX protein, humanHistone AcetyltransferasesHistonesKAT5 protein, humanLysineLysine Acetyltransferase 5PARP1 protein, humanPoly (ADP-Ribose) Polymerase-1

Identifiers

PMID26976643
PMCPMC4859686
OpenAlexW2345389685

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.