Evidence map›Paper›PMID 41190242›Full record

ArticleNAR cancer2025

Shining light on drug discovery: optogenetic screening for TopBP1 biomolecular condensate inhibitors.

Laura Morano, Nadia Vie, Adam Aissanou, Dana Hodroj, Véronique Garambois, Alexandra Fauvre, Alexy Promonet, Tom Egger, Benoît Bordignon, Cédric Hassen-Khodja and 4 more

Abstract read
In one paragraph

Article in NAR cancer, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Article
  2. 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

14 authors.

Laura MoranoIGH, Univ Montpellier, CNRS, Montpellier 3436, France.
Nadia VieInstitut de Recherche en Cancérologie de Montpellier, INSERM, CNRS, Univ Montpellier, Montpellier 34298, France.
Adam AissanouInstitut de Recherche en Cancérologie de Montpellier, INSERM, CNRS, Univ Montpellier, Montpellier 34298, France.
Dana HodrojIGH, Univ Montpellier, CNRS, Montpellier 3436, France.
Véronique GaramboisInstitut de Recherche en Cancérologie de Montpellier, INSERM, CNRS, Univ Montpellier, Montpellier 34298, France.
Alexandra FauvreInstitut de Recherche en Cancérologie de Montpellier, INSERM, CNRS, Univ Montpellier, Montpellier 34298, France.
Alexy PromonetIGH, Univ Montpellier, CNRS, Montpellier 3436, France.
Tom EggerIGH, Univ Montpellier, CNRS, Montpellier 3436, France.
Benoît BordignonMontpellier Ressources Imagerie BioCampus, Univ Montpellier, CNRS, INSERM, Montpellier 34298, France.ORCID 0000-0003-4977-3939
Cédric Hassen-KhodjaMontpellier Ressources Imagerie BioCampus, Univ Montpellier, CNRS, INSERM, Montpellier 34298, France.
Solène FiachettiIGH, Univ Montpellier, CNRS, Montpellier 3436, France.
Jihane BasbousIGH, Univ Montpellier, CNRS, Montpellier 3436, France.ORCID 0000-0002-3943-627X
Céline GongoraInstitut de Recherche en Cancérologie de Montpellier, INSERM, CNRS, Univ Montpellier, Montpellier 34298, France.
Angelos ConstantinouIGH, Univ Montpellier, CNRS, Montpellier 3436, France.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Human topoisomerase IIβ binding protein 1 (TopBP1) is a scaffold protein involved in DNA replication initiation, DNA repair, transcription regulation, and checkpoint activation. TopBP1 forms nuclear condensates that act as a molecular switch to amplify ATR activity and promote the activation of the checkpoint effector kinase Chk1. In cancer cells, ATR activity is crucial to tolerate the intrinsically high level of DNA lesions and obstacles that block replication fork progression. Thus, ATR inhibitors are currently tested in clinical trials, often in combination with chemotherapy drugs. However, resistance and toxicity are still major issues. The weak interactions that hold TopBP1 condensates together are highly sensitive to changes in the cellular milieu, suggesting that small molecules may alter the formation of TopBP1 condensates. Here, we developed a high-throughput screening system to identify TopBP1 condensation modulators. This system allowed us to identify FDA-approved drugs, including thimerosal and quinacrine, that inhibit TopBP1 condensation and block the activation of ATR/Chk1 signaling. Mechanistically, quinacrine impaired TopBP1's ability to associate with chromatin, thereby interfering with its capacity to form condensates. Furthermore, quinacrine enhanced the therapeutic efficacy of 5-fluorouracil and irinotecan, components of the clinically used FOLFIRI regimen in a mouse model of peritoneal carcinomatosis from colorectal cancer.

Indexed as

Antineoplastic AgentsCarrier ProteinsDNA-Binding ProteinsDrug DiscoveryNuclear ProteinsAnimalsAtaxia Telangiectasia Mutated ProteinsCell Line, TumorCheckpoint Kinase 1FluorouracilHigh-Throughput Screening AssaysHumansIrinotecanMiceSignal TransductionAntineoplastic AgentsAtaxia Telangiectasia Mutated ProteinsATR protein, humanCarrier ProteinsCheckpoint Kinase 1CHEK1 protein, humanDNA-Binding ProteinsFluorouracilIrinotecanNuclear ProteinsTOPBP1 protein, human

Identifiers

PMID41190242
PMCPMC12582362

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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.