Evidence map›Paper›PMID 39636933›Full record

ArticleScience (New York, N.Y.)2025

Molecular basis of FIGNL1 in dissociating RAD51 from DNA and chromatin.

Alexander Carver, Tai-Yuan Yu, Luke A Yates, Travis White, Raymond Wang, Katie Lister, Maria Jasin, Xiaodong Zhang

Abstract read
In one paragraph

Article in Science (New York, N.Y.), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
–field-weighted citation impact
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

12 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Mass Photometry Analysis of Membrane Proteins in Detergent Micelles.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  6. RAD51AP1 is a versatile RAD51 modulator.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Subunit specialization in AAA+ proteins and substrate unfolding during transcription complex remodeling.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  12. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors.

Alexander Carver *DNA Processing Machines Laboratory, Francis Crick Institute, London, UK.ORCID 0000-0003-0411-4817
Tai-Yuan Yu *Developmental Biology Program, Memorial Sloan Kettering Cancer Center, New York, USA.ORCID 0000-0001-5489-1150
Luke A YatesDNA Processing Machines Laboratory, Francis Crick Institute, London, UK.ORCID 0000-0002-5023-0803
Travis WhiteDevelopmental Biology Program, Memorial Sloan Kettering Cancer Center, New York, USA.ORCID 0000-0002-0069-5987
Raymond WangDevelopmental Biology Program, Memorial Sloan Kettering Cancer Center, New York, USA.ORCID 0000-0001-7611-626X
Katie ListerDNA Processing Machines Laboratory, Francis Crick Institute, London, UK.ORCID 0009-0002-3152-1151
Maria JasinDevelopmental Biology Program, Memorial Sloan Kettering Cancer Center, New York, USA.ORCID 0000-0002-7976-2379
Xiaodong ZhangDNA Processing Machines Laboratory, Francis Crick Institute, London, UK.ORCID 0000-0001-9786-7038

Funding

X-RAY CRYSTALLOGRAPHYP30CA008748 · NCI · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI SELWYN M VICKERS · 1985 to 2026
$347.4M
Homology-directed repair: BRCA2 and RAD51 paralogsR35CA253174 · NCI · SLOAN-KETTERING INST CAN RESEARCH · PI Maria Jasin · 2020 to 2026
$6.7M
NCI NIH HHS P30 CA008748NCI NIH HHS R35 CA253174Wellcome Trust 227769Wellcome Trust CC0103
6 · The paper itself

Abstract

Maintaining genome integrity is an essential and challenging process. RAD51 recombinase, the central component of several crucial processes in repairing DNA and protecting genome integrity, forms filaments on DNA, which are tightly regulated. One of these RAD51 regulators is FIGNL1 (fidgetin-like 1), which prevents RAD51 genotoxic chromatin association in normal cells and persistent RAD51 foci upon DNA damage. The cryogenic electron microscopy-imaged structure of FIGNL1 in complex with RAD51 reveals that FIGNL1 forms a nonplanar hexamer and encloses RAD51 N terminus in the FIGNL1 hexamer pore. Mutations in pore loop or catalytic residues of FIGNL1 render it defective in filament disassembly and are lethal in mouse embryonic stem cells. Our study reveals a distinct mechanism for removing RAD51 from bound substrates and provides the molecular basis for FIGNL1 in maintaining genome stability.

Indexed as

ATPases Associated with Diverse Cellular ActivitiesChromatinDNAMicrotubule-Associated ProteinsNuclear ProteinsRad51 RecombinaseAnimalsCell LineCryoelectron MicroscopyDNA DamageDNA RepairGenomic InstabilityHumansMiceMouse Embryonic Stem CellsMutationATPases Associated with Diverse Cellular ActivitiesChromatinDNAFIGNL1 protein, humanFIGNL1 protein, mouseMicrotubule-Associated ProteinsNuclear ProteinsRad51 protein, mouseRad51 Recombinase

Identifiers

PMID39636933
PMCPMC7617353

What OpenQuestion holds

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Registered trials

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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.