Evidence map›Paper›PMID 23751493›Full record

ArticleThe Journal of cell biology2013

RNF111/Arkadia is a SUMO-targeted ubiquitin ligase that facilitates the DNA damage response.

Sara L Poulsen, Rebecca K Hansen, Sebastian A Wagner, Loes van Cuijk, Gijsbert J van Belle, Werner Streicher, Mats Wikström, Chunaram Choudhary, Adriaan B Houtsmuller, Jurgen A Marteijn and 2 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of cell biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 100 papers.

0numbers the graph read from it
0cells of the map it votes in
100citing papers in PubMed
8.8field-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

100 citing papers in PubMed, 163 citations in OpenAlex.

  1. Review
  2. Article
  3. Immune regulation by the SUMO family.Nature reviews. Immunology · 2025
    Review
  4. Article
  5. Article
  6. Article
  7. Multifaceted roles of SUMO in DNA metabolism.Nucleus (Austin, Tex.) · 2024
    Review
  8. Article
  9. Article
  10. Article
  11. SUMO and the DNA damage response.Biochemical Society transactions · 2024
    Review
  12. Review
  13. Regulatory Effect ofPharmaceuticals (Basel, Switzerland) · 2023
    Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

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

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

12 authors at 5 institutions in 3 countries.

Sara L PoulsenUbiquitin Signaling Group, Department of Disease Biology, The Novo Nordisk Foundation Center for Protein Research, University of Copenhagen, DK-2200 Copenhagen, Denmark.
Rebecca K Hansen
Sebastian A Wagner
Loes van Cuijk
Gijsbert J van Belle
Werner Streicher
Mats Wikström
Chunaram Choudhary
Adriaan B Houtsmuller
Jurgen A Marteijn
Simon Bekker-Jensen
Niels Mailand
University of Copenhagen · DKPediatrics and Genetics · USNovo Nordisk Foundation · DKSterling Research Group · USMeertens Institute · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein modifications by ubiquitin and small ubiquitin-like modifier (SUMO) play key roles in cellular signaling pathways. SUMO-targeted ubiquitin ligases (STUbLs) directly couple these modifications by selectively recognizing SUMOylated target proteins through SUMO-interacting motifs (SIMs), promoting their K48-linked ubiquitylation and degradation. Only a single mammalian STUbL, RNF4, has been identified. We show that human RNF111/Arkadia is a new STUbL, which used three adjacent SIMs for specific recognition of poly-SUMO2/3 chains, and used Ubc13-Mms2 as a cognate E2 enzyme to promote nonproteolytic, K63-linked ubiquitylation of SUMOylated target proteins. We demonstrate that RNF111 promoted ubiquitylation of SUMOylated XPC (xeroderma pigmentosum C) protein, a central DNA damage recognition factor in nucleotide excision repair (NER) extensively regulated by ultraviolet (UV)-induced SUMOylation and ubiquitylation. Moreover, we show that RNF111 facilitated NER by regulating the recruitment of XPC to UV-damaged DNA. Our findings establish RNF111 as a new STUbL that directly links nonproteolytic ubiquitylation and SUMOylation in the DNA damage response.

Indexed as

Cell Line, TransformedDNA DamageDNA RepairHeLa CellsHumansLigasesNuclear ProteinsPlasmidsRNA, Small InterferingSignal TransductionSmall Ubiquitin-Related Modifier ProteinsSumoylationUbiquitinationUbiquitin-Conjugating EnzymesUbiquitin-Protein LigasesUbiquitinsLigasesNuclear ProteinsRNA, Small InterferingRNF111 protein, humanSmall Ubiquitin-Related Modifier ProteinsSUMO2 protein, humanSUMO3 protein, humanUBE2N protein, humanUBE2V2 protein, humanUbiquitin-Conjugating EnzymesUbiquitin-Protein LigasesUbiquitins

Identifiers

PMID23751493
PMCPMC3678163
OpenAlexW2151854650

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.