Evidence map›Paper›PMID 26438602›Full record

ArticleMolecular and cellular biology2015

Acetylation of Histone H2AX at Lys 5 by the TIP60 Histone Acetyltransferase Complex Is Essential for the Dynamic Binding of NBS1 to Damaged Chromatin.

Masae Ikura, Kanji Furuya, Shun Matsuda, Ryo Matsuda, Hiroki Shima, Jun Adachi, Tomonari Matsuda, Takuma Shiraki, Tsuyoshi Ikura

Open access · bronzeAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Molecular and cellular biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
1.7field-weighted citation impact, top 17% 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

37 citing papers in PubMed, 63 citations in OpenAlex.

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  19. Review
  20. Impact of NuclearMolecular and cellular biology · 2022
    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

9 authors at 4 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.
Shun MatsudaLaboratory of Environment Quality Management, Research Center for Environmental Quality Management, Kyoto University, Otsu, Shiga, Japan.
Ryo MatsudaLaboratory of Chromatin Regulatory Network, Department of Mutagenesis, Radiation Biology Center, Kyoto University, Kyoto, Japan.
Hiroki ShimaDepartment of Biochemistry, Tohoku University Graduate School of Medicine, Sendai, Japan.
Jun AdachiNational Institute of Biomedical Innovation, Ibaraki, Osaka, Japan.
Tomonari MatsudaLaboratory of Environment Quality Management, Research Center for Environmental Quality Management, Kyoto University, Otsu, Shiga, Japan.
Takuma ShirakiFaculty of Biology-Oriented Science and Technology, Kinki University, Wakayama, 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 · JPKindai University · JPNational Institute of Biomedical Innovation, Health and Nutrition · JPTohoku University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The association and dissociation of DNA damage response (DDR) factors with damaged chromatin occurs dynamically, which is crucial for the activation of DDR signaling in a spatiotemporal manner. We previously showed that the TIP60 histone acetyltransferase complex acetylates histone H2AX, to facilitate H2AX exchange at sites of DNA damage. However, it remained unclear how the acetylation of histone H2AX by TIP60 is related to the DDR signaling. We found that the acetylation but not the phosphorylation of H2AX is essential for the turnover of NBS1 on damaged chromatin. The loss of H2AX acetylation at Lys 5 by TIP60 in cells disturbed the accumulation of NBS1 at sites of DNA damage. Although the phosphorylation of H2AX is also reportedly required for the retention of NBS1 at damage sites, our data indicated that the acetylation-dependent NBS1 turnover by TIP60 on damaged chromatin restricts the dispersal of NBS1 foci from the sites of DNA damage. These findings indicate the importance of the acetylation-dependent dynamic binding of NBS1 to damaged chromatin, created by histone H2AX exchange, for the proper accumulation of NBS1 at DNA damage sites.

Indexed as

AcetylationAnimalsCell Cycle ProteinsCell Line, TumorCell NucleusChromatinDNADNA DamageDNA RepairHeLa CellsHistone AcetyltransferasesHistonesHumansLysine Acetyltransferase 5MiceMice, KnockoutCell Cycle ProteinsChromatinDNAH2AX protein, humanHistone AcetyltransferasesHistonesKAT5 protein, humanLysine Acetyltransferase 5NBN protein, humanNuclear ProteinsRNA, Small Interfering

Identifiers

PMID26438602
PMCPMC4648820
OpenAlexW1670992708

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.