Evidence map›Paper›PMID 40304182›Full record

ArticleNucleic acids research2025

CARM1/PRMT4 facilitates XPF-ERCC1 heterodimer assembly and maintains nucleotide excision repair activity.

Hiroyuki Niida, Masahiko Ito, Kenta Iijima, Akira Motegi, Rin Ogihara, Hironobu Akiyama, Chiharu Uchida, Satoshi Sakai, Tatsuya Ohhata, Atsushi Hatano and 5 more

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Article in Nucleic acids research, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

15 authors.

Hiroyuki NiidaDepartment of Molecular Biology, Hamamatsu University School of Medicine, 1-20-1 Handayama, Hamamatsu, Shizuoka 431-3192, Japan.ORCID 0000-0001-7508-055X
Masahiko ItoDepartment of Microbiology and Immunology, Hamamatsu University School of Medicine, Hamamatsu, Shizuoka 431-3192, Japan.
Kenta IijimaLaboratory Animal Facilities and Services, Institute of Photonics Medicine, Hamamatsu University School of Medicine, 1-20-1 Handayama, Hamamatsu, Shizuoka 431-3192, Japan.
Akira MotegiDepartment of Radiation Genetics, Kyoto University Graduate School of Medicine, Yoshida-Konoe-cho, Kyoto 606-8501, Japan.
Rin OgiharaDepartment of Molecular Biology, Hamamatsu University School of Medicine, 1-20-1 Handayama, Hamamatsu, Shizuoka 431-3192, Japan.
Hironobu AkiyamaDepartment of Molecular Biology, Hamamatsu University School of Medicine, 1-20-1 Handayama, Hamamatsu, Shizuoka 431-3192, Japan.
Chiharu UchidaAdvanced Research Facilities and Services, Institute of Photonics Medicine, Hamamatsu University School of Medicine, 1-20-1 Handayama, Hamamatsu, Shizuoka 431-3192, Japan.
Satoshi SakaiDepartment of Molecular Biology, Hamamatsu University School of Medicine, 1-20-1 Handayama, Hamamatsu, Shizuoka 431-3192, Japan.
Tatsuya OhhataDepartment of Molecular Biology, Hamamatsu University School of Medicine, 1-20-1 Handayama, Hamamatsu, Shizuoka 431-3192, Japan.
Atsushi HatanoDepartment of Omics and Systems Biology, Graduate School of Medical and Dental Sciences, Niigata University, Niigata 951-8510, Japan.
Michiko HiroseBioresource Engineering Division, RIKEN BioResource Research Center, Ibaraki 305-0074, Japan.
Atsuo OguraBioresource Engineering Division, RIKEN BioResource Research Center, Ibaraki 305-0074, Japan.ORCID 0000-0003-0447-1988
Masaki MatsumotoDepartment of Omics and Systems Biology, Graduate School of Medical and Dental Sciences, Niigata University, Niigata 951-8510, Japan.
Neil Q McDonaldInstitute of Structural and Molecular Biology, School of Natural Sciences, Birkbeck College, Malet Street, London WC1E 7HX, United Kingdom.
Masatoshi KitagawaDepartment of Molecular Biology, Hamamatsu University School of Medicine, 1-20-1 Handayama, Hamamatsu, Shizuoka 431-3192, Japan.ORCID 0000-0002-5819-048X

Funding

Cancer Research UK CC2068Medical Research Council CC2068Ministry of Education 16K08580Wellcome Trust CC2068
6 · The paper itself

Abstract

The structure-specific endonuclease, XPF-ERCC1, plays a central role in DNA damage repair. This nuclease is known to be important for nucleotide excision repair, interstrand crosslink repair, and DNA double-strand repair. We found that the arginine methyltransferase, CARM1/PRMT4, is essential for XPF stabilization and maintenance of intracellular protein levels. Loss of CARM1 results in a decrease in XPF protein levels and a concomitant decrease in ERCC1 protein. A similar destabilization of XPF protein was observed in cells expressing a mutant in which XPF arginine 568 was replaced by lysine. Loss of CARM1 impaired XPF-ERCC1 accumulation at the site of damage and delayed removal of cyclobutane pyrimidine dimers by UV. As a result, CARM1-deficient cells showed increased UV sensitivity. Our results provide insight into the importance of CARM1 not only in the mechanism of XPF-ERCC1 complex stabilization but also in the maintenance of genome stability.

Indexed as

DNA-Binding ProteinsDNA RepairEndonucleasesProtein-Arginine N-MethyltransferasesDNA DamageExcision RepairGenomic InstabilityHumansProtein MultimerizationPyrimidine DimersUltraviolet Rayscoactivator-associated arginine methyltransferase 1DNA-Binding ProteinsEndonucleasesERCC1 protein, humanProtein-Arginine N-MethyltransferasesPyrimidine Dimersxeroderma pigmentosum group F protein

Identifiers

PMID40304182
PMCPMC12041854

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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.