Evidence map›Paper›PMID 30177756›Full record

ArticleNature structural & molecular biology2018

The nuclear actin-containing Arp8 module is a linker DNA sensor driving INO80 chromatin remodeling.

Kilian R Knoll, Sebastian Eustermann, Vanessa Niebauer, Elisa Oberbeckmann, Gabriele Stoehr, Kevin Schall, Alessandro Tosi, Marianne Schwarz, Andrea Buchfellner, Philipp Korber and 1 more

Abstract read
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In one paragraph

Article in Nature structural & molecular biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
3.7field-weighted citation impact, top 6% 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

51 citing papers in PubMed, 92 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Recent advances in nuclear actin research.Nucleus (Austin, Tex.) · 2025
    Review
  7. Article
  8. Article
  9. Mechanistic insights into INO80-type chromatin remodelers.Current opinion in structural biology · 2025
    Review
  10. Article
  11. Article
  12. Article
  13. Structure of the human TIP60 complex.Nature communications · 2024
    Article
  14. Review
  15. Article
  16. Article
  17. Review
  18. Article
  19. 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

11 authors at 4 institutions in 1 country.

Kilian R KnollDepartment of Biochemistry, Ludwig-Maximilians-Universität München, Munich, Germany.
Sebastian EustermannDepartment of Biochemistry, Ludwig-Maximilians-Universität München, Munich, Germany.
Vanessa NiebauerDepartment of Biochemistry, Ludwig-Maximilians-Universität München, Munich, Germany.
Elisa OberbeckmannChair of Molecular Biology, Biomedical Center, Faculty of Medicine, Ludwig-Maximilians-Universität München, Munich, Germany.
Gabriele StoehrDepartment of Biochemistry, Ludwig-Maximilians-Universität München, Munich, Germany.
Kevin SchallDepartment of Biochemistry, Ludwig-Maximilians-Universität München, Munich, Germany.
Alessandro TosiDepartment of Biochemistry, Ludwig-Maximilians-Universität München, Munich, Germany.
Marianne SchwarzDepartment of Biochemistry, Ludwig-Maximilians-Universität München, Munich, Germany.
Andrea BuchfellnerChromoTek GmbH, Planegg, Germany.
Philipp KorberChair of Molecular Biology, Biomedical Center, Faculty of Medicine, Ludwig-Maximilians-Universität München, Munich, Germany.
Karl-Peter HopfnerDepartment of Biochemistry, Ludwig-Maximilians-Universität München, Munich, Germany. hopfner@genzentrum.lmu.de.ORCID http://orcid.org/0000-0002-4528-8357
Ludwig-Maximilians-Universität München · DECenter for Integrated Protein Science Munich · DEUniversität Ulm · DEUrologische Klinik München · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nuclear actin (N-actin) and actin-related proteins (Arps) are critical components of several chromatin modulating complexes, including the chromatin remodeler INO80, but their function is largely elusive. Here, we report the crystal structure of the 180-kDa Arp8 module of Saccharomyces cerevisiae INO80 and establish its role in recognition of extranucleosomal linker DNA. Arp8 engages N-actin in a manner distinct from that of other actin-fold proteins and thereby specifies recruitment of the Arp4-N-actin heterodimer to a segmented scaffold of the helicase-SANT-associated (HSA) domain of Ino80. The helical HSA domain spans over 120 Å and provides an extended binding platform for extranucleosomal entry DNA that is required for nucleosome sliding and genome-wide nucleosome positioning. Together with the recent cryo-electron microscopy structure of INO80

Indexed as

Chromatin Assembly and DisassemblyAmino Acid SequenceCell NucleusDNA, FungalMicrofilament ProteinsProtein ConformationSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence Homology, Amino AcidARP8 protein, S cerevisiaeDNA, FungalINO80 complex, S cerevisiaeMicrofilament ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID30177756
OpenAlexW2888742489

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.