Evidence map›Paper›PMID 20023648›Full record

ArticleNature cell biology2010

HERC2 coordinates ubiquitin-dependent assembly of DNA repair factors on damaged chromosomes.

Simon Bekker-Jensen, Jannie Rendtlew Danielsen, Kasper Fugger, Irina Gromova, Annika Nerstedt, Claudia Lukas, Jiri Bartek, Jiri Lukas, Niels Mailand

Erratum issuedAbstract read
PubMed Publisher
In one paragraph

Article in Nature cell biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 161 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
161citing papers in PubMed, 1 pooled it
14.1field-weighted citation impact, top 1% 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

161 citing papers in PubMed, 1 synthesis or guideline pooled it, 272 citations in OpenAlex.

  1. Pooled it
  2. Genome-wide association study identifies a genetic variant associated with risk for more aggressive prostate cancer.Cancer epidemiology, biomarkers & prevention : a publication of the American Association for Cancer Research, cosponsored by the American Society of Preventive Oncology · 2011
    Trial
  3. Article
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  11. Mechanistic insights into the iron-sulfur cluster-dependent interaction of the autophagy receptor NCOA4 with the E3 ligase HERC2.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  12. Article
  13. Article
  14. Review
  15. SUMO and the DNA damage response.Biochemical Society transactions · 2024
    Review
  16. Review
  17. Review
  18. Article
  19. Article
  20. Article

101 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

  • Erratum issued
    Lukas, Claudia [added]
5 · Who and what money

Authors and funding

9 authors at 2 institutions in 1 country.

Simon Bekker-JensenCentre for Genotoxic Stress Research, Department of Proteomics in Cancer, Institute of Cancer Biology, Danish Cancer Society, Copenhagen, Denmark.
Jannie Rendtlew Danielsen
Kasper Fugger
Irina Gromova
Annika Nerstedt
Claudia Lukas
Jiri Bartek
Jiri Lukas
Niels Mailand
University of Copenhagen · DKDanish Cancer Society · DK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Regulatory ubiquitylation is emerging as an important mechanism to protect genome integrity in cells exposed to DNA damage. However, the spectrum of known ubiquitin regulators of the DNA damage response (DDR) is limited and their functional interplay is poorly understood. Here, we identify HERC2 as a factor that regulates ubiquitin-dependent retention of repair proteins on damaged chromosomes. In response to ionising radiation (IR), HERC2 forms a complex with RNF8, a ubiquitin ligase involved in the DDR. The HERC2-RNF8 interaction requires IR-inducible phosphorylation of HERC2 at Thr 4827, which in turn binds to the forkhead-associated (FHA) domain of RNF8. Mechanistically, we provide evidence that HERC2 facilitates assembly of the ubiquitin-conjugating enzyme Ubc13 with RNF8, thereby promoting DNA damage-induced formation of Lys 63-linked ubiquitin chains. We also show that HERC2 interacts with, and maintains the levels of, RNF168, another ubiquitin ligase operating downstream of RNF8 (Refs 7, 8). Consequently, knockdown of HERC2 abrogates ubiquitin-dependent retention of repair factors such as 53BP1, RAP80 and BRCA1. Together with the increased radiosensitivity of HERC2-depleted cells, these results uncover a regulatory layer in the orchestration of protein interactions on damaged chromosomes and they underscore the role of ubiquitin-mediated signalling in genome maintenance.

Indexed as

DNA RepairBone NeoplasmsBRCA1 ProteinCarrier ProteinsCells, CulturedChromosomes, HumanDNA-Binding ProteinsDNA DamageGuanine Nucleotide Exchange FactorsHistone ChaperonesHumansIntracellular Signaling Peptides and ProteinsKidneyLysineMutationNuclear ProteinsBRCA1 ProteinBRCA1 protein, humanCarrier ProteinsDNA-Binding ProteinsGuanine Nucleotide Exchange FactorsHERC2 protein, humanHistone ChaperonesIntracellular Signaling Peptides and ProteinsLysineNuclear ProteinsRNA, Small InterferingRNF8 protein, humanTP53BP1 protein, humanTumor Suppressor p53-Binding Protein 1UbiquitinUbiquitin-Protein LigasesUIMC1 protein, human

Identifiers

PMID20023648
OpenAlexW2091073356

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.