Evidence map›Paper›PMID 23115235›Full record

ArticleThe Journal of biological chemistry2012

The RING finger protein RNF8 ubiquitinates Nbs1 to promote DNA double-strand break repair by homologous recombination.

Chi-Sheng Lu, Lan N Truong, Aaron Aslanian, Linda Z Shi, Yongjiang Li, Patty Yi-Hwa Hwang, Kwi Hye Koh, Tony Hunter, John R Yates, Michael W Berns and 1 more

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed, 1 pooled it
–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

37 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
  2. Review
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  5. Article
  6. Crystal structure of the folded domains of Xrs2 from Saccharomyces cerevisiae.Acta crystallographica. Section F, Structural biology communications · 2025
    Article
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  17. Beyond K48 and K63: non-canonical protein ubiquitination.Cellular & molecular biology letters · 2021
    Review
  18. Article
  19. Article
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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

11 authors.

Chi-Sheng LuDepartment of Molecular and Experimental Medicine, Scripps Research Institute, La Jolla, California 92037, USA.
Lan N Truong
Aaron Aslanian
Linda Z Shi
Yongjiang Li
Patty Yi-Hwa Hwang
Kwi Hye Koh
Tony Hunter
John R Yates
Michael W Berns
Xiaohua Wu

Funding

ZDS2P REGULATES SWE1P-DEPENDENT POLARIZED CELL GROWTH IN S CEREVISIAEP41RR011823 · NCRR · UNIVERSITY OF WASHINGTON · PI SALVESEN, GUY S. · 1996 to 2011
$24.7M
TrainingP41GM103533 · NIGMS · UNIVERSITY OF WASHINGTON · PI MACCOSS, MICHAEL · 2012 to 2021
$20.7M
SOMATIC CELL CYCLE REGULATION BY PHOSPHORYLATIONR01CA080100 · NCI · SALK INSTITUTE FOR BIOLOGICAL STUDIES · PI HUNTER, TONY R. · 1999 to 2018
$13.1M
Role of the Mre11/Rad50/Nbs1 complex in DNA damage response pathwaysR01CA102361 · NCI · SCRIPPS RESEARCH INSTITUTE, THE · PI WU, XIAOHUA · 2003 to 2012
$4.1M
S-phase checkpoint and rereplication in mammalian cellsR01GM080677 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI WU, XIAOHUA · 2010 to 2018
$2.9M
Role of BRCA1 and its association protein CtlP in DNA double-strand break repairR01CA140972 · NCI · SCRIPPS RESEARCH INSTITUTE, THE · PI WU, XIAOHUA · 2010 to 2014
$2.2M
NCI NIH HHS CA102361NCI NIH HHS CA102361-07S1NCI NIH HHS CA140972NCI NIH HHS CA80100NCI NIH HHS R01 CA080100NCI NIH HHS R01 CA102361NCI NIH HHS R01 CA140972NCRR NIH HHS P41 RR011823NIGMS NIH HHS GM080677NIGMS NIH HHS P41 GM103533NIGMS NIH HHS R01 GM080677
6 · The paper itself

Abstract

Ubiquitination plays an important role in the DNA damage response. We identified a novel interaction of the E3 ubiquitin ligase RNF8 with Nbs1, a key regulator of DNA double-strand break (DSB) repair. We found that Nbs1 is ubiquitinated both before and after DNA damage and is a direct ubiquitination substrate of RNF8. We also identified key residues on Nbs1 that are ubiquitinated by RNF8. By using laser microirradiation and live-cell imaging, we observed that RNF8 and its ubiquitination activity are important for promoting optimal binding of Nbs1 to DSB-containing chromatin. We also demonstrated that RNF8-mediated ubiquitination of Nbs1 contributes to the efficient and stable binding of Nbs1 to DSBs and is important for HR-mediated DSB repair. Taken together, these studies suggest that Nbs1 is one important target of RNF8 to regulate DNA DSB repair.

Indexed as

DNA Breaks, Double-StrandedCell Cycle ProteinsCell Line, TumorDNA-Binding ProteinsDNA RepairHomologous RecombinationHumansLasersNuclear ProteinsUbiquitinationUbiquitin-Protein LigasesCell Cycle ProteinsDNA-Binding ProteinsNBN protein, humanNuclear ProteinsRNF8 protein, humanUbiquitin-Protein Ligases

Identifiers

PMID23115235
PMCPMC3527981

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.