Evidence map›Paper›PMID 32204557›Full record

ArticleCells2020

The Actin-Family Protein Arp4 Is a Novel Suppressor for the Formation and Functions of Nuclear F-Actin.

Shota Yamazaki, Christian Gerhold, Koji Yamamoto, Yuya Ueno, Robert Grosse, Kei Miyamoto, Masahiko Harata

Open access · goldAbstract read
In one paragraph

Article in Cells, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.0field-weighted citation impact, top 28% 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

9 citing papers in PubMed, 14 citations in OpenAlex.

  1. Recent advances in nuclear actin research.Nucleus (Austin, Tex.) · 2025
    Review
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Envisioning a role for nuclear actin in prophase I spermatocytes.Frontiers in cell and developmental biology · 2023
    Review
  8. Article
  9. 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

7 authors at 4 institutions in 3 countries.

Shota YamazakiLaboratory of Molecular Biology, Graduate School of Agricultural Science, Tohoku University, Sendai 980-0845, Japan.ORCID 0000-0003-2209-3351
Christian GerholdFriedrich-Miescher Institute for Biomedical Research, Maulbeerstr. 66, 4058 Basel, Switzerland.
Koji YamamotoLaboratory of Molecular Biology, Graduate School of Agricultural Science, Tohoku University, Sendai 980-0845, Japan.
Yuya UenoLaboratory of Molecular Biology, Graduate School of Agricultural Science, Tohoku University, Sendai 980-0845, Japan.
Robert GrosseInstitute of Experimental and Clinical Pharmakology and Toxicology, Faculty of Medicine, University of Freiburg, Alberstrasse 25, 79104 Freiburg, Germany.ORCID 0000-0002-3380-5273
Kei MiyamotoLaboratory of Molecular Developmental Biology, Faculty of Biology-Oriented Science and Technology, Kindai University, Wakayama 649-6493, Japan.
Masahiko HarataLaboratory of Molecular Biology, Graduate School of Agricultural Science, Tohoku University, Sendai 980-0845, Japan.
Tohoku University · JPFriedrich Miescher Institute · CHKindai University · JPUniversity of Freiburg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The crosstalk between actin and actin-related proteins (Arps), namely Arp2 and Arp3, plays a central role in facilitating actin polymerization in the cytoplasm and also in the nucleus. Nuclear F-actin is required for transcriptional regulation, double-strand break repair, and nuclear organization. The formation of nuclear F-actin is highly dynamic, suggesting the involvement of positive and negative regulators for nuclear actin polymerization. While actin assembly factors for nuclear F-actin have been recently described, information about inhibitory factors is still limited. The actin-related protein Arp4 which is predominantly localized in the nucleus, has been previously identified as an integral subunit of multiple chromatin modulation complexes, where it forms a heterodimer with monomeric actin. Therefore, we tested whether Arp4 functions as a suppressor of nuclear F-actin formation. The knockdown of Arp4 (Arp4 KD) led to an increase in nuclear F-actin formation in NIH3T3 cells, and purified Arp4 potently inhibited F-actin formation in mouse nuclei transplanted into

Indexed as

ActinsAnimalsCell NucleusChromosomal Proteins, Non-HistoneDNA-Binding ProteinsDNA Breaks, Double-StrandedDNA RepairGene Expression RegulationMiceNIH 3T3 CellsOocytesTranscription, GeneticWnt Signaling PathwayXenopusActinsActl6a protein, mouseChromosomal Proteins, Non-HistoneDNA-Binding Proteinsactin-related proteinepigeneticsnuclear actinnuclear architecturenucleoskeleton

Identifiers

PMID32204557
PMCPMC7140684
OpenAlexW3011660455

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.