Evidence map›Paper›PMID 31390569›Full record

ArticleCell reports2019

Nej1 Interacts with Mre11 to Regulate Tethering and Dna2 Binding at DNA Double-Strand Breaks.

Aditya Mojumdar, Kyle Sorenson, Marcel Hohl, Mathias Toulouze, Susan P Lees-Miller, Karine Dubrana, John H J Petrini, Jennifer A Cobb

Open access · goldAbstract read
In one paragraph

Article in Cell reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
2.0field-weighted citation impact, top 13% 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

16 citing papers in PubMed, 33 citations in OpenAlex.

  1. Review
  2. Rap1-mediated steric hindrance protects telomeres from MRX sensing.Nature structural & molecular biology · 2026
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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

8 authors at 4 institutions in 3 countries.

Aditya MojumdarDepartments of Biochemistry and Molecular Biology and Oncology, Robson DNA Science Centre, Arnie Charbonneau Cancer Institute, Cumming School of Medicine, University of Calgary, 3330 Hospital Drive N.W., Calgary AB T2N 4N1, Canada.
Kyle SorensonDepartments of Biochemistry and Molecular Biology and Oncology, Robson DNA Science Centre, Arnie Charbonneau Cancer Institute, Cumming School of Medicine, University of Calgary, 3330 Hospital Drive N.W., Calgary AB T2N 4N1, Canada.
Marcel HohlMolecular Biology Program, Memorial Sloan Kettering Cancer Center, New York, NY 10065, USA.
Mathias ToulouzeLaboratoire Instabilité et Organisation Nucléaire, iRCM, Commissariat à l'Énergie Atomique et aux Énergies Alternatives (CEA)/Direction de la Recherche Fondamentale (DRF), U1274, Institut National de la Santé et de la Recherche Médicale (INSERM), UMR1274, Université Paris-Diderot et Université Paris-Sud, 92260 Fontenay-aux-Roses Cedex, France.
Susan P Lees-MillerDepartments of Biochemistry and Molecular Biology and Oncology, Robson DNA Science Centre, Arnie Charbonneau Cancer Institute, Cumming School of Medicine, University of Calgary, 3330 Hospital Drive N.W., Calgary AB T2N 4N1, Canada.
Karine DubranaLaboratoire Instabilité et Organisation Nucléaire, iRCM, Commissariat à l'Énergie Atomique et aux Énergies Alternatives (CEA)/Direction de la Recherche Fondamentale (DRF), U1274, Institut National de la Santé et de la Recherche Médicale (INSERM), UMR1274, Université Paris-Diderot et Université Paris-Sud, 92260 Fontenay-aux-Roses Cedex, France.
John H J PetriniMolecular Biology Program, Memorial Sloan Kettering Cancer Center, New York, NY 10065, USA.
Jennifer A CobbDepartments of Biochemistry and Molecular Biology and Oncology, Robson DNA Science Centre, Arnie Charbonneau Cancer Institute, Cumming School of Medicine, University of Calgary, 3330 Hospital Drive N.W., Calgary AB T2N 4N1, Canada. Electronic address: jcobb@ucalgary.ca.
University of Calgary · CAMemorial Sloan Kettering Cancer Center · USDirection de la Recherche Fondamentale · FRUniversité Paris-Sud · FR

Funding

X-RAY CRYSTALLOGRAPHYP30CA008748 · NCI · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI Hongbiao Carl Lekaye · 1985 to 2026
$347.4M
ROLES OF MRELL AND RAD50 IN THE DNA DAMAGE RESPONSER01GM056888 · NIGMS · UNIVERSITY OF WISCONSIN MADISON · PI PETRINI, JOHN HJ · 1998 to 2019
$8.6M
DNA Damage & DNA Replication: a Complex RelationshipR35GM136278 · NIGMS · SLOAN-KETTERING INST CAN RESEARCH · PI John HJ Petrini · 2020 to 2026
$5.5M
Regulation of the DNA damage response by the Mre11 complexR37GM059413 · NIGMS · SLOAN-KETTERING INST CAN RESEARCH · PI PETRINI, JOHN HJ · 2012 to 2020
$5.2M
CIHR MOP-13639CIHR MOP-137062CIHR MOP-82736NCI NIH HHS P30 CA008748NIGMS NIH HHS R01 GM056888NIGMS NIH HHS R35 GM136278NIGMS NIH HHS R37 GM059413
6 · The paper itself

Abstract

Non-homologous end joining (NHEJ) and homologous recombination (HR) are the two major pathways of DNA double-strand break (DSB) repair and both are highly conserved from yeast to mammals. Nej1 has a role in DNA end-tethering at a DSB, and the Mre11/Rad50/Xrs2 (MRX) complex is important for its recruitment to the break. Nej1 and Dna2-Sgs1 interact with the C-terminal end of Mre11, which also includes the region where Rad50 binds. By characterizing the functionality of Nej1 in two rad50 mutants, which alter the structural features of MRX, we demonstrate that Nej1 inhibits the binding of Dna2 to Mre11 and Sgs1. Nej1 interactions with Mre11 promote tethering and inhibit hyper-resection, and when these events are compromised, large deletions develop at a DSB. The work indicates that Nej1 provides a layer of regulation to repair pathway choice and is consistent with its role in NHEJ.

Indexed as

DNA Breaks, Double-StrandedDNA RepairDNA-Binding ProteinsDNA, FungalDNA HelicasesEndodeoxyribonucleasesExodeoxyribonucleasesMultiprotein ComplexesRecQ HelicasesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsDNA2 protein, S cerevisiaeDNA-Binding ProteinsDNA, FungalDNA HelicasesEndodeoxyribonucleasesExodeoxyribonucleasesMRE11 protein, S cerevisiaeMultiprotein ComplexesNEJ1 protein, S cerevisiaeRecQ HelicasesSaccharomyces cerevisiae ProteinsSGS1 protein, S cerevisiae5′ resectionDSB repairend-tetheringMre11-Rad50-Xrs2MRXNej1NHEJ

Identifiers

PMID31390569
PMCPMC6746346
OpenAlexW2944728517

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.