Dual roles of the DHX9 RGG domain in hybrid-dependent recruitment and suppression of 53BP1.

Yuina Tsuchiya, Yudai Hiwatashi, Hayaki Ikegame, Saaya Matsuya, Yurina Abe, Ryotaro Nishi

Abstract read

In one paragraph

Article in Scientific reports, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it

0cells of the map it votes in

0citing 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

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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

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0 citing papers in PubMed.

No citing paper in PubMed yet.

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.

Yuina TsuchiyaGraduate School of Bionics, Tokyo University of Technology, Hachioji, Tokyo, 192-0982, Japan.

Yudai HiwatashiGraduate School of Bionics, Tokyo University of Technology, Hachioji, Tokyo, 192-0982, Japan.

Hayaki IkegameGraduate School of Bionics, Tokyo University of Technology, Hachioji, Tokyo, 192-0982, Japan.

Saaya MatsuyaGraduate School of Bionics, Tokyo University of Technology, Hachioji, Tokyo, 192-0982, Japan.

Yurina AbeGraduate School of Bionics, Tokyo University of Technology, Hachioji, Tokyo, 192-0982, Japan.

Ryotaro NishiGraduate School of Bionics, Tokyo University of Technology, Hachioji, Tokyo, 192-0982, Japan. nishirtr@stf.teu.ac.jp.

Funding

Japan Society for the Promotion of Science 21K12244

6 · The paper itself

Abstract

DNA double-strand breaks (DSBs) are repaired mainly by non-homologous end-joining (NHEJ) and homologous recombination repair (HR) in mammalian cells. Recent studies highlight the importance of RNA in regulating these pathways and influencing pathway choice, particularly through the formation and resolution of DNA-RNA hybrids. Here, we show that DNA-RNA hybrids are formed at DSB sites in a PARP1- and poly (ADP-ribosyl)ation-dependent manner and are resolved by DHX9 dependent manner. The carboxyl-terminal RGG domain of DHX9 is necessary and sufficient for its recruitment and is required for efficient DNA end-resection. We further identify methylated arginine residues within this domain that are required for suppressing loading of the NHEJ-promoting factor 53BP1 to the DSB sites. Our findings highlight a central role of the RGG domain of DHX9 in DNA-RNA hybrid regulation and DSB repair pathway choice.

Indexed as

DEAD-box RNA HelicasesNeoplasm ProteinsTumor Suppressor p53-Binding Protein 1DNADNA Breaks, Double-StrandedDNA End-Joining RepairHumansPoly (ADP-Ribose) Polymerase-1Protein DomainsRNADEAD-box RNA HelicasesDHX9 protein, humanDNANeoplasm ProteinsPoly (ADP-Ribose) Polymerase-1RNATP53BP1 protein, humanTumor Suppressor p53-Binding Protein 1

Identifiers

PMID42332175

DOI10.1038/s41598-026-59280-6

PMCPMC13575197

What OpenQuestion holds

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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.