Evidence map›Paper›PMID 31417085›Full record

ArticleNature communications2019

Arkadia/RNF111 is a SUMO-targeted ubiquitin ligase with preference for substrates marked with SUMO1-capped SUMO2/3 chain.

Annie M Sriramachandran, Katrin Meyer-Teschendorf, Stefan Pabst, Helle D Ulrich, Niels H Gehring, Kay Hofmann, Gerrit J K Praefcke, R Jürgen Dohmen

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
3.3field-weighted citation impact, top 7% 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

53 citing papers in PubMed, 76 citations in OpenAlex.

  1. Article
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  9. Review
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  13. Article
  14. SUMO Antibody Validation.Methods in molecular biology (Clifton, N.J.) · 2025
    Article
  15. The SUMO Pathway.Methods in molecular biology (Clifton, N.J.) · 2025
    Review
  16. Review
  17. Multifaceted roles of SUMO in DNA metabolism.Nucleus (Austin, Tex.) · 2024
    Review
  18. Article
  19. Article
  20. Review
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 2 institutions in 1 country.

Annie M SriramachandranInstitute for Genetics, Faculty of Mathematics and Natural Sciences, University of Cologne, Center of Molecular Biosciences, Zülpicher Str. 47a, D-50674, Cologne, Germany.
Katrin Meyer-TeschendorfInstitute for Genetics, Faculty of Mathematics and Natural Sciences, University of Cologne, Center of Molecular Biosciences, Zülpicher Str. 47a, D-50674, Cologne, Germany.
Stefan PabstInstitute for Genetics, Faculty of Mathematics and Natural Sciences, University of Cologne, Center of Molecular Biosciences, Zülpicher Str. 47a, D-50674, Cologne, Germany.ORCID http://orcid.org/0000-0003-1073-4246
Helle D UlrichInstitute of Molecular Biology, Ackermannweg 4, D-55128, Mainz, Germany.ORCID http://orcid.org/0000-0003-0431-2223
Niels H GehringInstitute for Genetics, Faculty of Mathematics and Natural Sciences, University of Cologne, Center of Molecular Biosciences, Zülpicher Str. 47a, D-50674, Cologne, Germany.ORCID http://orcid.org/0000-0001-7792-1164
Kay HofmannInstitute for Genetics, Faculty of Mathematics and Natural Sciences, University of Cologne, Center of Molecular Biosciences, Zülpicher Str. 47a, D-50674, Cologne, Germany. Kay.Hofmann@uni-koeln.de.ORCID http://orcid.org/0000-0002-2289-9083
Gerrit J K PraefckeInstitute for Genetics, Faculty of Mathematics and Natural Sciences, University of Cologne, Center of Molecular Biosciences, Zülpicher Str. 47a, D-50674, Cologne, Germany. Gerrit.Praefcke@pei.de.
R Jürgen DohmenInstitute for Genetics, Faculty of Mathematics and Natural Sciences, University of Cologne, Center of Molecular Biosciences, Zülpicher Str. 47a, D-50674, Cologne, Germany. j.dohmen@uni-koeln.de.ORCID http://orcid.org/0000-0002-5756-6780
University of Cologne · DEInstitute of Molecular Biology · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Modification with SUMO regulates many eukaryotic proteins. Down-regulation of sumoylated forms of proteins involves either their desumoylation, and hence recycling of the unmodified form, or their proteolytic targeting by ubiquitin ligases that recognize their SUMO modification (termed STUbL or ULS). STUbL enzymes such as Uls1 and Slx5-Slx8 in budding yeast or RNF4 and Arkadia/RNF111 in humans bear multiple SUMO interaction motifs to recognize substrates carrying poly-SUMO chains. Using yeast as experimental system and isothermal titration calorimetry, we here show that Arkadia specifically selects substrates carrying SUMO1-capped SUMO2/3 hybrid conjugates and targets them for proteasomal degradation. Our data suggest that a SUMO1-specific binding site in Arkadia with sequence similarity to a SUMO1-binding site in DPP9 is required for targeting endogenous hybrid SUMO conjugates and PML nuclear bodies in human cells. We thus characterize Arkadia as a STUbL with a preference for substrate proteins marked with distinct hybrid SUMO chains.

Indexed as

SumoylationEscherichia coliHeLa CellsHumansNuclear ProteinsProteasome Endopeptidase ComplexProteolysisSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSmall Ubiquitin-Related Modifier ProteinsSUMO-1 ProteinUbiquitinationUbiquitin-Protein LigasesUbiquitinsNuclear ProteinsProteasome Endopeptidase ComplexRNF111 protein, humanSaccharomyces cerevisiae ProteinsSlx5 protein, S cerevisiaeSmall Ubiquitin-Related Modifier ProteinsSUMO-1 ProteinSUMO1 protein, humanSUMO2 protein, humanSUMO3 protein, humanUbiquitin-Protein LigasesUbiquitins

Identifiers

PMID31417085
PMCPMC6695498
OpenAlexW2968185949

What OpenQuestion holds

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LicenceCC BY
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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.