Evidence map›Paper›PMID 26524493›Full record

ArticleNature structural & molecular biology2015

A new vertebrate SUMO enzyme family reveals insights into SUMO-chain assembly.

Nathalie Eisenhardt, Viduth K Chaugule, Stefanie Koidl, Mathias Droescher, Esen Dogan, Jan Rettich, Päivi Sutinen, Susumu Y Imanishi, Kay Hofmann, Jorma J Palvimo and 1 more

Abstract read
PubMed Publisher
In one paragraph

Article in Nature structural & molecular biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 69 papers.

0numbers the graph read from it
0cells of the map it votes in
69citing papers in PubMed
–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

69 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Review
  6. Article
  7. Solo or in Concert: SUMOylation in Pathogenic Fungi.The plant pathology journal · 2025
    Review
  8. Article
  9. Review
  10. Article
  11. Review
  12. The SUMO Pathway.Methods in molecular biology (Clifton, N.J.) · 2025
    Review
  13. Article
  14. Production and Purification of SUMO-UBC9 and SUMO-RANGAP1Methods in molecular biology (Clifton, N.J.) · 2025
    Article
  15. Article
  16. Multifaceted roles of SUMO in DNA metabolism.Nucleus (Austin, Tex.) · 2024
    Review
  17. Article
  18. Article
  19. Article
  20. Review

9 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

11 authors.

Nathalie EisenhardtDepartment of Epigenetics, Max Planck Institute of Immunobiology and Epigenetics, Freiburg, Germany.
Viduth K ChauguleDepartment of Epigenetics, Max Planck Institute of Immunobiology and Epigenetics, Freiburg, Germany.
Stefanie KoidlDepartment of Epigenetics, Max Planck Institute of Immunobiology and Epigenetics, Freiburg, Germany.
Mathias DroescherDepartment of Epigenetics, Max Planck Institute of Immunobiology and Epigenetics, Freiburg, Germany.
Esen DoganDepartment of Epigenetics, Max Planck Institute of Immunobiology and Epigenetics, Freiburg, Germany.ORCID http://orcid.org/0000-0003-0558-145X
Jan RettichDepartment of Epigenetics, Max Planck Institute of Immunobiology and Epigenetics, Freiburg, Germany.
Päivi SutinenInstitute of Biomedicine, University of Eastern Finland, Kuopio, Finland.
Susumu Y ImanishiTurku Centre for Biotechnology, University of Turku and Åbo Akademi University, Turku, Finland.ORCID http://orcid.org/0000-0002-3641-4390
Kay HofmannInstitute for Genetics, University of Cologne, Cologne, Germany.ORCID http://orcid.org/0000-0002-2289-9083
Jorma J PalvimoInstitute of Biomedicine, University of Eastern Finland, Kuopio, Finland.
Andrea PichlerDepartment of Epigenetics, Max Planck Institute of Immunobiology and Epigenetics, Freiburg, Germany.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

SUMO chains act as stress-induced degradation tags or repair factor-recruiting signals at DNA lesions. Although E1 activating, E2 conjugating and E3 ligating enzymes efficiently assemble SUMO chains, specific chain-elongation mechanisms are unknown. E4 elongases are specialized E3 ligases that extend a chain but are inefficient in the initial conjugation of the modifier. We identified ZNF451, a representative member of a new class of SUMO2 and SUMO3 (SUMO2/3)-specific enzymes that execute catalysis via a tandem SUMO-interaction motif (SIM) region. One SIM positions the donor SUMO while a second SIM binds SUMO on the back side of the E2 enzyme. This tandem-SIM region is sufficient to extend a back side-anchored SUMO chain (E4 elongase activity), whereas efficient chain initiation also requires a zinc-finger region to recruit the initial acceptor SUMO (E3 ligase activity). Finally, we describe four human proteins sharing E4 elongase activities and their function in stress-induced SUMO2/3 conjugation.

Indexed as

Protein MultimerizationAnimalsHumansSmall Ubiquitin-Related Modifier ProteinsVertebratesSmall Ubiquitin-Related Modifier Proteins

Identifiers

PMID26524493

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.