Evidence map›Paper›PMID 33453169›Full record

ArticleMolecular cell2021

RADX controls RAD51 filament dynamics to regulate replication fork stability.

Madison B Adolph, Taha M Mohamed, Swati Balakrishnan, Chaoyou Xue, Florian Morati, Mauro Modesti, Eric C Greene, Walter J Chazin, David Cortez

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

23 citing papers in PubMed, 36 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Review
  10. RAD52 prevents accumulation ofbioRxiv : the preprint server for biology · 2024
    Article
  11. Structure of RADX and mechanism for regulation of RAD51 nucleofilaments.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  12. Article
  13. Article
  14. Article
  15. Structure of RADX and mechanism for regulation of RAD51 nucleofilaments.bioRxiv : the preprint server for biology · 2023
    Article
  16. Article
  17. Zinc Finger MYND-Type Containing 8 (ZMYND8) Is Epigenetically Regulated in Mutant Isocitrate Dehydrogenase 1 (IDH1) Glioma to Promote Radioresistance.Clinical cancer research : an official journal of the American Association for Cancer Research · 2023
    Article
  18. Article
  19. Review
  20. Review
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

9 authors at 3 institutions in 2 countries.

Madison B AdolphDepartment of Biochemistry, Vanderbilt University School of Medicine, Nashville, TN, USA.
Taha M MohamedDepartment of Biochemistry, Vanderbilt University School of Medicine, Nashville, TN, USA.
Swati BalakrishnanDepartment of Biochemistry, Vanderbilt University School of Medicine, Nashville, TN, USA; Center for Structural Biology, Vanderbilt University School of Medicine, Nashville, TN, USA.
Chaoyou XueDepartment of Biochemistry and Molecular Biophysics, Columbia University, New York, NY USA.
Florian MoratiCancer Research Center of Marseille, CNRS UMR7258, Inserm U1068, Institut Paoli-Calmettes, Aix-Marseille Université U105, Marseille, France.
Mauro ModestiCancer Research Center of Marseille, CNRS UMR7258, Inserm U1068, Institut Paoli-Calmettes, Aix-Marseille Université U105, Marseille, France.
Eric C GreeneDepartment of Biochemistry and Molecular Biophysics, Columbia University, New York, NY USA.
Walter J ChazinDepartment of Biochemistry, Vanderbilt University School of Medicine, Nashville, TN, USA; Center for Structural Biology, Vanderbilt University School of Medicine, Nashville, TN, USA. Electronic address: walter.j.chazin@vanderbilt.edu.
David CortezDepartment of Biochemistry, Vanderbilt University School of Medicine, Nashville, TN, USA. Electronic address: david.cortez@vanderbilt.edu.
Vanderbilt University · USCentre National de la Recherche Scientifique · FRColumbia University · US

Funding

Transcription-Coupled & Replication-Associated Excision RepairP01CA092584 · NCI · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI WALTER J. CHAZIN · 2001 to 2026
$89.6M
Analysis of the Replication Stress ResponseR01GM116616 · NIGMS · VANDERBILT UNIVERSITY · PI David K Cortez · 2015 to 2026
$5.4M
Structural Biology of Multi-Domain Proteins and Multi-Protein Machinery in DNA Replication and RepairR35GM118089 · NIGMS · VANDERBILT UNIVERSITY · PI WALTER J. CHAZIN · 2016 to 2026
$4.9M
Defining the contributions of BRCA1, BRCA2, and RAD52 to genome stabilityR01CA221858 · NCI · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI GREENE, ERIC C · 2020 to 2024
$1.9M
NCI NIH HHS P01 CA092584NCI NIH HHS R01 CA221858NIGMS NIH HHS R01 GM116616NIGMS NIH HHS R35 GM118089
6 · The paper itself

Abstract

The RAD51 recombinase forms nucleoprotein filaments to promote double-strand break repair, replication fork reversal, and fork stabilization. The stability of these filaments is highly regulated, as both too little and too much RAD51 activity can cause genome instability. RADX is a single-strand DNA (ssDNA) binding protein that regulates DNA replication. Here, we define its mechanism of action. We find that RADX inhibits RAD51 strand exchange and D-loop formation activities. RADX directly and selectively interacts with ATP-bound RAD51, stimulates ATP hydrolysis, and destabilizes RAD51 nucleofilaments. The RADX interaction with RAD51, in addition to its ssDNA binding capability, is required to maintain replication fork elongation rates and fork stability. Furthermore, BRCA2 can overcome the RADX-dependent RAD51 inhibition. Thus, RADX functions in opposition to BRCA2 in regulating RAD51 nucleofilament stability to ensure the right level of RAD51 function during DNA replication.

Indexed as

DNA ReplicationAdenosine TriphosphateBRCA2 ProteinCell Line, TumorDNADNA-Binding ProteinsDNA, Single-StrandedFibroblastsGene Expression RegulationGenes, ReporterGreen Fluorescent ProteinsHEK293 CellsHumansHydrolysisLuminescent ProteinsRad51 RecombinaseAdenosine TriphosphateBRCA2 ProteinBRCA2 protein, humanDNADNA-Binding ProteinsDNA, Single-StrandedGreen Fluorescent ProteinsLuminescent ProteinsRAD51 protein, humanRad51 RecombinaseRADX protein, humanRed Fluorescent ProteinRNA-Binding ProteinsDNA curtainDNA damage responseDNA repairdouble-strand breakelectron microscopyfork reversalreplication stress

Identifiers

PMID33453169
PMCPMC7935748
OpenAlexW3118624412

What OpenQuestion holds

Textmetadata
LicenceTDM
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.