Evidence map›Paper›PMID 37891173›Full record

ArticleNature communications2023

FIGNL1 AAA+ ATPase remodels RAD51 and DMC1 filaments in pre-meiotic DNA replication and meiotic recombination.

Masaru Ito, Asako Furukohri, Kenichiro Matsuzaki, Yurika Fujita, Atsushi Toyoda, Akira Shinohara

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
4.8field-weighted citation impact, top 4% 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

13 citing papers in PubMed, 31 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Distinct and interdependent functions of three RING proteins regulate recombination during mammalian meiosis.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Molecular basis of FIGNL1 in dissociating RAD51 from DNA and chromatin.bioRxiv : the preprint server for biology · 2024
    Article
  13. 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

6 authors at 3 institutions in 1 country.

Masaru ItoInstitute for Protein Research, Osaka University, Suita, Osaka, 565-0871, Japan. msrito2@protein.osaka-u.ac.jp.ORCID 0000-0002-7478-5002
Asako FurukohriInstitute for Protein Research, Osaka University, Suita, Osaka, 565-0871, Japan.ORCID 0000-0002-4329-6978
Kenichiro MatsuzakiInstitute for Protein Research, Osaka University, Suita, Osaka, 565-0871, Japan.ORCID 0009-0005-7375-7658
Yurika FujitaInstitute for Protein Research, Osaka University, Suita, Osaka, 565-0871, Japan.
Atsushi ToyodaAdvanced Genomics Center, National Institute of Genetics, Mishima, Shizuoka, 411-8540, Japan.ORCID 0000-0002-0728-7548
Akira ShinoharaInstitute for Protein Research, Osaka University, Suita, Osaka, 565-0871, Japan. ashino@protein.osaka-u.ac.jp.ORCID 0000-0003-4207-8247
Protein Research Foundation · JPNara University · JPNational Institute of Genetics · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The formation of RAD51/DMC1 filaments on single-stranded (ss)DNAs essential for homology search and strand exchange in DNA double-strand break (DSB) repair is tightly regulated. FIGNL1 AAA+++ ATPase controls RAD51-mediated recombination in human cells. However, its role in gametogenesis remains unsolved. Here, we characterized a germ line-specific conditional knockout (cKO) mouse of FIGNL1. Fignl1 cKO male mice showed defective chromosome synapsis and impaired meiotic DSB repair with the accumulation of RAD51/DMC1 on meiotic chromosomes, supporting a positive role of FIGNL1 in homologous recombination at a post-assembly stage of RAD51/DMC1 filaments. Fignl1 cKO spermatocytes also accumulate RAD51/DMC1 on chromosomes in pre-meiotic S-phase. These RAD51/DMC1 assemblies are independent of meiotic DSB formation. We also showed that purified FIGNL1 dismantles RAD51 filament on double-stranded (ds)DNA as well as ssDNA. These results suggest an additional role of FIGNL1 in limiting the non-productive assembly of RAD51/DMC1 on native dsDNAs during pre-meiotic S-phase and meiotic prophase I.

Indexed as

MeiosisRad51 RecombinaseAnimalsATPases Associated with Diverse Cellular ActivitiesCell Cycle ProteinsDNADNA-Binding ProteinsDNA Breaks, Double-StrandedDNA ReplicationHomologous RecombinationHumansMaleMiceMicrotubule-Associated ProteinsNuclear ProteinsATPases Associated with Diverse Cellular ActivitiesCell Cycle ProteinsDMC1 protein, humanDNADNA-Binding ProteinsFIGNL1 protein, humanMicrotubule-Associated ProteinsNuclear ProteinsRAD51 protein, humanRad51 Recombinase

Identifiers

PMID37891173
PMCPMC10611733
OpenAlexW4387975702

What OpenQuestion holds

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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.