Evidence map›Paper›PMID 25299602›Full record

ArticlePloS one2014

DNA binding properties of the actin-related protein Arp8 and its role in DNA repair.

Akihisa Osakabe, Yuichiro Takahashi, Hirokazu Murakami, Kenji Otawa, Hiroaki Tachiwana, Yukako Oma, Hitoshi Nishijima, Kei-ich Shibahara, Hitoshi Kurumizaka, Masahiko Harata

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
0.9field-weighted citation impact, top 27% 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

14 citing papers in PubMed, 22 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Envisioning a role for nuclear actin in prophase I spermatocytes.Frontiers in cell and developmental biology · 2023
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. The INO80 remodeller in transcription, replication and repair.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2017
    Review
  12. Article
  13. Review
  14. 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

10 authors at 4 institutions in 2 countries.

Akihisa OsakabeLaboratory of Structural Biology, Graduate School of Advanced Science and Engineering, Waseda University, Tokyo, Japan.
Yuichiro TakahashiLaboratory of Molecular Biology, Graduate School of Agricultural Science, Tohoku University, Sendai, Japan.
Hirokazu MurakamiLaboratory of Molecular Biology, Graduate School of Agricultural Science, Tohoku University, Sendai, Japan.
Kenji OtawaLaboratory of Structural Biology, Graduate School of Advanced Science and Engineering, Waseda University, Tokyo, Japan.
Hiroaki TachiwanaLaboratory of Structural Biology, Graduate School of Advanced Science and Engineering, Waseda University, Tokyo, Japan.
Yukako OmaLaboratory of Molecular Biology, Graduate School of Agricultural Science, Tohoku University, Sendai, Japan.
Hitoshi NishijimaDepartment of Integrated Genetics, National Institute of Genetics, Mishima, Japan.
Kei-ich ShibaharaDepartment of Integrated Genetics, National Institute of Genetics, Mishima, Japan.
Hitoshi KurumizakaLaboratory of Structural Biology, Graduate School of Advanced Science and Engineering, Waseda University, Tokyo, Japan.
Masahiko HarataLaboratory of Molecular Biology, Graduate School of Agricultural Science, Tohoku University, Sendai, Japan.
Waseda University · JPMRC Laboratory of Molecular Biology · GBNational Institute of Genetics · JPTohoku University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Actin and actin-related proteins (Arps), which are members of the actin family, are essential components of many of these remodeling complexes. Actin, Arp4, Arp5, and Arp8 are found to be evolutionarily conserved components of the INO80 chromatin remodeling complex, which is involved in transcriptional regulation, DNA replication, and DNA repair. A recent report showed that Arp8 forms a module in the INO80 complex and this module can directly capture a nucleosome. In the present study, we showed that recombinant human Arp8 binds to DNAs, and preferentially binds to single-stranded DNA. Analysis of the binding of adenine nucleotides to Arp8 mutants suggested that the ATP-binding pocket, located in the evolutionarily conserved actin fold, plays a regulatory role in the binding of Arp8 to DNA. To determine the cellular function of Arp8, we derived tetracycline-inducible Arp8 knockout cells from a cultured human cell line. Analysis of results obtained after treating these cells with aphidicolin and camptothecin revealed that Arp8 is involved in DNA repair. Together with the previous observation that Arp8, but not γ-H2AX, is indispensable for recruiting INO80 complex to DSB in human, results of our study suggest an individual role for Arp8 in DNA repair.

Indexed as

ActinsCell Line, TumorChromatin Assembly and DisassemblyDNA-Binding ProteinsDNA RepairDNA ReplicationDNA, Single-StrandedHumansMicrofilament ProteinsActinsACTR8 protein, humanDNA-Binding ProteinsDNA, Single-StrandedMicrofilament Proteins

Identifiers

PMID25299602
PMCPMC4191963
OpenAlexW2039025259

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.