Evidence map›Paper›PMID 34853311›Full record

ArticleNature communications2021

Structural basis for the E3 ligase activity enhancement of yeast Nse2 by SUMO-interacting motifs.

Nathalia Varejão, Jara Lascorz, Joan Codina-Fabra, Gemma Bellí, Helena Borràs-Gas, Jordi Torres-Rosell, David Reverter

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.9field-weighted citation impact, top 13% 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

25 citing papers in PubMed, 32 citations in OpenAlex.

  1. Review
  2. Article
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  6. Review
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  8. Article
  9. Chemical Tools for Probing the Ub/Ubl Conjugation Cascades.Chembiochem : a European journal of chemical biology · 2025
    Review
  10. Article
  11. Production and Purification of SUMO-UBC9 and SUMO-RANGAP1Methods in molecular biology (Clifton, N.J.) · 2025
    Article
  12. In Vitro SUMOylation Assays with a DNA-Sensitive Multi-subunit E3 Ligase.Methods in molecular biology (Clifton, N.J.) · 2025
    Article
  13. Multifaceted roles of SUMO in DNA metabolism.Nucleus (Austin, Tex.) · 2024
    Review
  14. Article
  15. Review
  16. Article
  17. Article
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  19. Review
  20. Article
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

7 authors at 2 institutions in 1 country.

Nathalia Varejão *Institut de Biotecnologia i de Biomedicina (IBB) and Dept. de Bioquímica i Biologia Molecular, Universitat Autònoma de Barcelona, 08193, Bellaterra, Spain.ORCID 0000-0002-6952-8896
Jara Lascorz *Institut de Biotecnologia i de Biomedicina (IBB) and Dept. de Bioquímica i Biologia Molecular, Universitat Autònoma de Barcelona, 08193, Bellaterra, Spain.ORCID 0000-0002-5823-0728
Joan Codina-FabraIRBLLEIDA, Dept. Ciències Mèdiques Bàsiques, Universitat de Lleida, Lleida, Spain.ORCID 0000-0002-6147-618X
Gemma BellíIRBLLEIDA, Dept. Ciències Mèdiques Bàsiques, Universitat de Lleida, Lleida, Spain.ORCID 0000-0002-4161-3204
Helena Borràs-GasInstitut de Biotecnologia i de Biomedicina (IBB) and Dept. de Bioquímica i Biologia Molecular, Universitat Autònoma de Barcelona, 08193, Bellaterra, Spain.
Jordi Torres-RosellIRBLLEIDA, Dept. Ciències Mèdiques Bàsiques, Universitat de Lleida, Lleida, Spain.ORCID 0000-0003-1308-6926
David ReverterInstitut de Biotecnologia i de Biomedicina (IBB) and Dept. de Bioquímica i Biologia Molecular, Universitat Autònoma de Barcelona, 08193, Bellaterra, Spain. david.reverter@uab.cat.ORCID 0000-0002-5347-0992
Universitat Autònoma de Barcelona · ESUniversitat de Lleida · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Post-translational modification of proteins by ubiquitin and ubiquitin-like modifiers, such as SUMO, are key events in protein homeostasis or DNA damage response. Smc5/6 is a nuclear multi-subunit complex that participates in the recombinational DNA repair processes and is required in the maintenance of chromosome integrity. Nse2 is a subunit of the Smc5/6 complex that possesses SUMO E3 ligase activity by the presence of a SP-RING domain that activates the E2~SUMO thioester for discharge on the substrate. Here we present the crystal structure of the SUMO E3 ligase Nse2 in complex with an E2-SUMO thioester mimetic. In addition to the interface between the SP-RING domain and the E2, the complex reveals how two SIM (SUMO-Interacting Motif) -like motifs in Nse2 are restructured upon binding the donor and E2-backside SUMO during the E3-dependent discharge reaction. Both SIM interfaces are essential in the activity of Nse2 and are required to cope with DNA damage.

Indexed as

Basic Helix-Loop-Helix ProteinsBiomimeticsCell Cycle ProteinsCrystallography, X-RayDNA DamageProtein Processing, Post-TranslationalProteostasisRecombinational DNA RepairRepressor ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSmall Ubiquitin-Related Modifier ProteinsUbiquitinUbiquitinationUbiquitin-Protein LigasesBasic Helix-Loop-Helix ProteinsCell Cycle ProteinsRepressor ProteinsSaccharomyces cerevisiae ProteinsSIM1 protein, S cerevisiaeSmall Ubiquitin-Related Modifier ProteinsSMC5 protein, S cerevisiaeUbiquitinUbiquitin-Protein Ligases

Identifiers

PMID34853311
PMCPMC8636563
OpenAlexW3214860800

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.