Evidence map›Paper›PMID 27895153›Full record

ArticleMolecular and cellular biology2017

Ubiquitylation of Ku80 by RNF126 Promotes Completion of Nonhomologous End Joining-Mediated DNA Repair.

Noriko Ishida, Tadashi Nakagawa, Shun-Ichiro Iemura, Akira Yasui, Hiroki Shima, Yasutake Katoh, Yuko Nagasawa, Toru Natsume, Kazuhiko Igarashi, Keiko Nakayama

Open access · bronzeAbstract read
In one paragraph

Article in Molecular and cellular biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

42 citing papers in PubMed, 65 citations in OpenAlex.

  1. Review
  2. Article
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  4. Review
  5. The functional landscape of the human ubiquitinome.bioRxiv : the preprint server for biology · 2025
    Article
  6. Article
  7. Article
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  10. Review
  11. Identification of the main barriers to Ku accumulation in chromatin.bioRxiv : the preprint server for biology · 2024
    Article
  12. Review
  13. Article
  14. Review
  15. Article
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  17. Review
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  19. Article
  20. A Novel Role for RNF126 in the Promotion of G2 Arrest via Interaction With 14-3-3σ.International journal of radiation oncology, biology, physics · 2022
    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

10 authors at 2 institutions in 1 country.

Noriko IshidaDivision of Cell Proliferation, ART, Graduate School of Medicine, Tohoku University, Sendai, Miyagi, Japan.
Tadashi NakagawaDivision of Cell Proliferation, ART, Graduate School of Medicine, Tohoku University, Sendai, Miyagi, Japan.
Shun-Ichiro IemuraBiomedical Information Research Center, National Institute of Advanced Industrial Science and Technology, Tokyo, Japan.
Akira YasuiDivision of Dynamic Proteome in Cancer and Aging, Institute of Development, Aging, and Cancer, Tohoku University, Sendai, Miyagi, Japan.
Hiroki ShimaDepartment of Biochemistry, Tohoku University Graduate School of Medicine, Sendai, Miyagi, Japan.
Yasutake KatohDepartment of Biochemistry, Tohoku University Graduate School of Medicine, Sendai, Miyagi, Japan.
Yuko NagasawaDivision of Cell Proliferation, ART, Graduate School of Medicine, Tohoku University, Sendai, Miyagi, Japan.
Toru NatsumeBiomedical Information Research Center, National Institute of Advanced Industrial Science and Technology, Tokyo, Japan.
Kazuhiko IgarashiDepartment of Biochemistry, Tohoku University Graduate School of Medicine, Sendai, Miyagi, Japan.
Keiko NakayamaDivision of Cell Proliferation, ART, Graduate School of Medicine, Tohoku University, Sendai, Miyagi, Japan nakayak2@med.tohoku.ac.jp.
Tohoku University · JPNational Institute of Advanced Industrial Science and Technology · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Repair of damaged DNA is critical for maintenance of genetic information. In eukaryotes, DNA double-strand breaks (DSBs) are recognized by the Ku70-Ku80 heterodimer, which then recruits proteins that mediate repair by nonhomologous end joining (NHEJ). Prolonged retention of Ku70/80 at DSBs prevents completion of repair, however, with ubiquitylation of Ku80 having been implicated in Ku70/80 dissociation from DNA. Here, we identify RNF126 as a ubiquitin ligase that is recruited to DSBs and ubiquitylates Ku80, with UBE2D3 serving as an E2 enzyme. Knockdown of RNF126 prevented Ku70/80 dissociation from DSBs and inhibited break repair. Attenuation of Ku80 ubiquitylation by replacement of ubiquitylation site lysines with arginine residues delayed Ku70/80 release from chromatin after DSB induction by genotoxic insults. Together, our data indicate that RNF126 is a novel regulator of NHEJ that promotes completion of DNA repair by ubiquitylating Ku80 and releasing Ku70/80 from damaged DNA.

Indexed as

DNA End-Joining RepairUbiquitinationAnimalsChromatinDNA Breaks, Double-StrandedHEK293 CellsHeLa CellsHumansKu AutoantigenMiceModels, BiologicalNIH 3T3 CellsProtein MultimerizationProteolysisRadiation, IonizingUbiquitin-Protein LigasesChromatinKu AutoantigenRNF126 protein, humanUbiquitin-Protein LigasesDNA repairKu80nonhomologous end joining (NHEJ)RNF126ubiquitylation

Identifiers

PMID27895153
PMCPMC5288581
OpenAlexW2559189553

What OpenQuestion holds

Textmetadata
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.