Evidence map›Paper›PMID 30388237›Full record

ArticleJournal of molecular cell biology2019

Structure and functional interactions of INO80 actin/Arp module.

Xuan Zhang, Xuejuan Wang, Zhihui Zhang, Gang Cai

Open access · hybridAbstract read
In one paragraph

Article in Journal of molecular cell biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.1field-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

19 citing papers in PubMed, 27 citations in OpenAlex.

  1. The Role of Arp2/3 in End-Resection During DNA Double-Strand Break Repair.BioEssays : news and reviews in molecular, cellular and developmental biology · 2026
    Review
  2. Article
  3. Recent advances in nuclear actin research.Nucleus (Austin, Tex.) · 2025
    Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Envisioning a role for nuclear actin in prophase I spermatocytes.Frontiers in cell and developmental biology · 2023
    Review
  9. Article
  10. Article
  11. Nuclear Actin Dynamics in Gene Expression, DNA Repair, and Cancer.Results and problems in cell differentiation · 2022
    Article
  12. Review
  13. Article
  14. Review
  15. Review
  16. Review
  17. Article
  18. Assembling nuclear domains: Lessons from DNA repair.The Journal of cell biology · 2019
    Review
  19. Nuclear actin switch of the INO80 remodeler.Journal of molecular cell biology · 2019
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Xuan ZhangHefei National Laboratory for Physical Sciences at Microscale and School of Life Sciences, University of Science & Technology of China, Hefei, China.
Xuejuan WangHefei National Laboratory for Physical Sciences at Microscale and School of Life Sciences, University of Science & Technology of China, Hefei, China.
Zhihui ZhangHefei National Laboratory for Physical Sciences at Microscale and School of Life Sciences, University of Science & Technology of China, Hefei, China.
Gang CaiHefei National Laboratory for Physical Sciences at Microscale and School of Life Sciences, University of Science & Technology of China, Hefei, China.
University of Science and Technology of China · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The presence and functions of nuclear actin have been controversial due to the lack of molecular mechanisms. Nuclear actin and actin-related proteins (Arps) are subunits of several chromatin remodelers, including the evolutionarily conserved INO80 chromatin-remodeling complex. Here, we present an improved cryo-EM structure of the yeast INO80 complex and the first 3D reconstruction of the INO80 actin/Arp module. The modular and subunit architecture is defined using a combination of subunit deletion analysis and published crosslinking-mass spectrometry. The functional interactions of the INO80 actin/Arp module with a nucleosome is 3D EM reconstructed in two different binding states. Nucleosomes initially bind to the Arp8 subunit and the substantial conformational changes maximize nucleosome contacts of the actin/Arp module, which could promote the bound nucleosome to be engaged onto the INO80 ATPase domain. Our findings suggest that the conserved nuclear actin/Arp module acts a conformational switch of the INO80 for nucleosome binding.

Indexed as

Cryoelectron MicroscopyImage Processing, Computer-AssistedMicrofilament ProteinsMolecular Dynamics SimulationMutationNucleosomesProtein BindingProtein DomainsProtein Structure, QuaternaryProtein SubunitsRecombinant ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsARP8 protein, S cerevisiaeINO80 complex, S cerevisiaeMicrofilament ProteinsNucleosomesProtein SubunitsRecombinant ProteinsSaccharomyces cerevisiae Proteinsactin/Arp–Nuc207 assemblyINO80modular architecturenuclear actin/Arp module

Identifiers

PMID30388237
PMCPMC6548343
OpenAlexW2899072610

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.