Evidence map›Paper›PMID 30022091›Full record

ArticleScientific reports2018

MDC1 methylation mediated by lysine methyltransferases EHMT1 and EHMT2 regulates active ATM accumulation flanking DNA damage sites.

Sugiko Watanabe, Makoto Iimori, David Virya Chan, Eiji Hara, Hiroyuki Kitao, Yoshihiko Maehara

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

11 citing papers in PubMed, 19 citations in OpenAlex.

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  9. Screen identifies DYRK1B network as mediator of transcription repression on damaged chromatin.Proceedings of the National Academy of Sciences of the United States of America · 2020
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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 at 2 institutions in 1 country.

Sugiko WatanabeInnovative Anticancer Strategy for Therapeutics and Diagnosis Group, Innovation Center for Medical Redox Navigation, Kyushu University, Fukuoka, 812-8582, Japan. sugikow@biken.osaka-u.ac.jp.ORCID 0000-0002-2120-9546
Makoto IimoriInnovative Anticancer Strategy for Therapeutics and Diagnosis Group, Innovation Center for Medical Redox Navigation, Kyushu University, Fukuoka, 812-8582, Japan.
David Virya ChanDepartment of Molecular Microbiology, Research Institute for Microbial Diseases, Osaka University, Suita, Osaka, 565-0871, Japan.ORCID 0000-0002-6817-2832
Eiji HaraDepartment of Molecular Microbiology, Research Institute for Microbial Diseases, Osaka University, Suita, Osaka, 565-0871, Japan.
Hiroyuki KitaoInnovative Anticancer Strategy for Therapeutics and Diagnosis Group, Innovation Center for Medical Redox Navigation, Kyushu University, Fukuoka, 812-8582, Japan. hkitao@phar.kyushu-u.ac.jp.ORCID 0000-0001-8682-2889
Yoshihiko MaeharaInnovative Anticancer Strategy for Therapeutics and Diagnosis Group, Innovation Center for Medical Redox Navigation, Kyushu University, Fukuoka, 812-8582, Japan.
Kyushu University · JPThe University of Osaka · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Chromatin dynamics mediated by post-translational modifications play a crucial role in cellular response to genotoxic stress for the maintenance of genome integrity. MDC1 is a pivotal chromatin adaptor in DNA damage response (DDR) and its methylation is essential to recruit repair factors at DNA double-strand break (DSB) sites, yet their precise molecular mechanisms remain elusive. Here we identified euchromatic histone-lysine N-methyltransferase 1 (EHMT1) and EHMT2 as novel regulators of MDC1, which is required for the accumulation of DDR factors e.g. 53BP1 and RAP80, at the DSB sites. MDC1 interacts mainly with EHMT1, which is facilitated by DNA damage-initiated ATM signalling, and EHMT2 dominantly modulates methylation of MDC1 lysine 45. This regulatory modification promotes the interaction between MDC1 and ATM to expand activated ATM on damaged chromatin and dysfunctional telomere. These findings identify EHMT1 and EHMT2 as DDR components, with implications for genome-integrity maintenance through proper dynamic methylation of MDC1.

Indexed as

DNA DamageDNA MethylationAdaptor Proteins, Signal TransducingAtaxia Telangiectasia Mutated ProteinsCell Cycle ProteinsChromatinDNA RepairGenomic InstabilityHistocompatibility AntigensHistone-Lysine N-MethyltransferaseHistonesHumansLysineNeoplasmsNuclear ProteinsTrans-ActivatorsAdaptor Proteins, Signal TransducingAtaxia Telangiectasia Mutated ProteinsATM protein, humanCell Cycle ProteinsChromatinEHMT1 protein, humanEHMT2 protein, humanHistocompatibility AntigensHistone-Lysine N-MethyltransferaseHistonesLysineMDC1 protein, humanNuclear ProteinsTrans-Activators

Identifiers

PMID30022091
PMCPMC6052104
OpenAlexW2879724978

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.