Evidence map›Paper›PMID 29095668›Full record

ArticleNucleus (Austin, Tex.)2018

SUMO modification system facilitates the exchange of histone variant H2A.Z-2 at DNA damage sites.

Atsuhiko Fukuto, Masae Ikura, Tsuyoshi Ikura, Jiying Sun, Yasunori Horikoshi, Hiroki Shima, Kazuhiko Igarashi, Masayuki Kusakabe, Masahiko Harata, Naoki Horikoshi and 3 more

Abstract read
In one paragraph

Article in Nucleus (Austin, Tex.), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
–field-weighted citation impact
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

16 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. SUMO and the DNA damage response.Biochemical Society transactions · 2024
    Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Review
  11. The histone variant H2A.Z in gene regulation.Epigenetics & chromatin · 2019
    Review
  12. Preserving genome integrity and function: the DNA damage response and histone modifications.Critical reviews in biochemistry and molecular biology · 2019
    Review
  13. Review
  14. Targeting Chromatin Remodeling for Cancer Therapy.Current molecular pharmacology · 2019
    Review
  15. Review
  16. Review
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

13 authors.

Atsuhiko Fukutoa Department of Cellular Biology , Research Institute for Radiation Biology and Medicine, Hiroshima University , Hiroshima , Japan.
Masae Ikurac Laboratory of Chromatin Regulatory Network, Department of Mutagenesis , Radiation Biology Center, Kyoto University , Kyoto , Japan.
Tsuyoshi Ikurac Laboratory of Chromatin Regulatory Network, Department of Mutagenesis , Radiation Biology Center, Kyoto University , Kyoto , Japan.
Jiying Suna Department of Cellular Biology , Research Institute for Radiation Biology and Medicine, Hiroshima University , Hiroshima , Japan.
Yasunori Horikoshia Department of Cellular Biology , Research Institute for Radiation Biology and Medicine, Hiroshima University , Hiroshima , Japan.
Hiroki Shimad Department of Biochemistry , Tohoku University Graduate School of Medicine , Sendai , Miyagi , Japan.
Kazuhiko Igarashid Department of Biochemistry , Tohoku University Graduate School of Medicine , Sendai , Miyagi , Japan.
Masayuki Kusakabee Laboratory of Molecular Biology, Graduate School of Agricultural Science , Tohoku University , Sendai , Miyagi , Japan.
Masahiko Haratae Laboratory of Molecular Biology, Graduate School of Agricultural Science , Tohoku University , Sendai , Miyagi , Japan.
Naoki Horikoshif Laboratory of Structural Biology, Graduate School of Advanced Science and Engineering , Waseda University, Shinjukuku , Tokyo , Japan.
Hitoshi Kurumizakaf Laboratory of Structural Biology, Graduate School of Advanced Science and Engineering , Waseda University, Shinjukuku , Tokyo , Japan.
Yoshiaki Kiuchib Department of Ophthalmology and Visual Science , Graduate School of Biomedical Sciences, Hiroshima University , Hiroshima , Japan.
Satoshi Tashiroa Department of Cellular Biology , Research Institute for Radiation Biology and Medicine, Hiroshima University , Hiroshima , Japan.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Histone exchange and histone post-translational modifications play important roles in the regulation of DNA metabolism, by re-organizing the chromatin configuration. We previously demonstrated that the histone variant H2A.Z-2 is rapidly exchanged at damaged sites after DNA double strand break induction in human cells. In yeast, the small ubiquitin-like modifier (SUMO) modification of H2A.Z is involved in the DNA damage response. However, whether the SUMO modification regulates the exchange of human H2A.Z-2 at DNA damage sites remains unclear. Here, we show that H2A.Z-2 is SUMOylated in a damage-dependent manner, and the SUMOylation of H2A.Z-2 is suppressed by the depletion of the SUMO E3 ligase, PIAS4. Moreover, PIAS4 depletion represses the incorporation and eviction of H2A.Z-2 at damaged sites. These findings demonstrate that the PIAS4-mediated SUMOylation regulates the exchange of H2A.Z-2 at DNA damage sites.

Indexed as

DNA DamageDNAHeLa CellsHistonesHumansProtein Processing, Post-TranslationalSUMO-1 ProteinDNAHistonesSUMO-1 ProteinDNA damageH2A.Z-2histone variantPIAS4SUMO

Identifiers

PMID29095668
PMCPMC5973225

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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.