Evidence map›Paper›PMID 34728620›Full record

ArticleNature communications2021

Arginine methylation and ubiquitylation crosstalk controls DNA end-resection and homologous recombination repair.

Maria Pilar Sanchez-Bailon, Soo-Youn Choi, Elizabeth R Dufficy, Karan Sharma, Gavin S McNee, Emma Gunnell, Kelly Chiang, Debashish Sahay, Sarah Maslen, Grant S Stewart and 3 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.4field-weighted citation impact, top 10% 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

26 citing papers in PubMed, 44 citations in OpenAlex.

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  15. Role of PRMT1 and PRMT5 in Breast Cancer.International journal of molecular sciences · 2024
    Review
  16. Article
  17. Decoding Ubiquitin Modifications by Mass Spectrometry.Advances in experimental medicine and biology · 2024
    Review
  18. Review
  19. Review
  20. Article
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

13 authors at 4 institutions in 2 countries.

Maria Pilar Sanchez-Bailon *Institute of Cancer and Genomic Sciences, University of Birmingham, Birmingham, UK.ORCID 0000-0001-6929-2273
Soo-Youn Choi *Institute of Cancer and Genomic Sciences, University of Birmingham, Birmingham, UK.
Elizabeth R Dufficy *Institute of Cancer and Genomic Sciences, University of Birmingham, Birmingham, UK.
Karan SharmaInstitute of Cancer and Genomic Sciences, University of Birmingham, Birmingham, UK.
Gavin S McNeeInstitute of Cancer and Genomic Sciences, University of Birmingham, Birmingham, UK.
Emma GunnellBiodiscovery Institute, School of Pharmacy, University of Nottingham, Nottingham, UK.
Kelly ChiangInstitute of Cancer and Genomic Sciences, University of Birmingham, Birmingham, UK.
Debashish SahayInstitute of Cancer and Genomic Sciences, University of Birmingham, Birmingham, UK.
Sarah MaslenMRC Laboratory of Molecular Biology, Cambridge, UK.ORCID 0000-0002-0261-2866
Grant S StewartInstitute of Cancer and Genomic Sciences, University of Birmingham, Birmingham, UK.ORCID 0000-0002-0960-3241
J Mark SkehelMRC Laboratory of Molecular Biology, Cambridge, UK.ORCID 0000-0002-2432-0901
Ingrid DrevenyBiodiscovery Institute, School of Pharmacy, University of Nottingham, Nottingham, UK.ORCID 0000-0003-2256-642X
Clare C DaviesInstitute of Cancer and Genomic Sciences, University of Birmingham, Birmingham, UK. c.c.davies@bham.ac.uk.ORCID 0000-0003-3097-1791
University of Birmingham · GBMRC Laboratory of Molecular Biology · GBUniversity of Nottingham · GBMax Delbrück Center · DE

Funding

Cancer Research UK 25500Cancer Research UK C17183/A23303Cancer Research UK C52376/A25500Medical Research Council 1501569Medical Research Council MC_U105184326Medical Research Council MR/M009912/1
6 · The paper itself

Abstract

Cross-talk between distinct protein post-translational modifications is critical for an effective DNA damage response. Arginine methylation plays an important role in maintaining genome stability, but how this modification integrates with other enzymatic activities is largely unknown. Here, we identify the deubiquitylating enzyme USP11 as a previously uncharacterised PRMT1 substrate, and demonstrate that the methylation of USP11 promotes DNA end-resection and the repair of DNA double strand breaks (DSB) by homologous recombination (HR), an event that is independent from another USP11-HR activity, the deubiquitylation of PALB2. We also show that PRMT1 is a ubiquitylated protein that it is targeted for deubiquitylation by USP11, which regulates the ability of PRMT1 to bind to and methylate MRE11. Taken together, our findings reveal a specific role for USP11 during the early stages of DSB repair, which is mediated through its ability to regulate the activity of the PRMT1-MRE11 pathway.

Indexed as

Recombinational DNA RepairUbiquitinationArginineCell LineDNA DamageGenomic InstabilityHumansMethylationMRE11 Homologue ProteinProtein-Arginine N-MethyltransferasesRad51 RecombinaseRepressor ProteinsThiolester HydrolasesArginineMRE11 Homologue ProteinMRE11 protein, humanPRMT1 protein, humanProtein-Arginine N-MethyltransferasesRAD51 protein, humanRad51 RecombinaseRepressor ProteinsThiolester HydrolasesUSP11 protein, human

Identifiers

PMID34728620
PMCPMC8564520
OpenAlexW3208000318

What OpenQuestion holds

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LicenceCC BY
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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.