Evidence map›Paper›PMID 25533188›Full record

ArticleMolecular cell2015

The SLX4 complex is a SUMO E3 ligase that impacts on replication stress outcome and genome stability.

Jean-Hugues Guervilly, Arato Takedachi, Valeria Naim, Sarah Scaglione, Charly Chawhan, Yoann Lovera, Emmanuelle Despras, Isao Kuraoka, Patricia Kannouche, Filippo Rosselli and 1 more

Open access · bronzeAbstract read
PubMed Publisher
In one paragraph

Article in Molecular cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 96 papers.

0numbers the graph read from it
0cells of the map it votes in
96citing papers in PubMed
7.7field-weighted citation impact, top 2% 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

96 citing papers in PubMed, 135 citations in OpenAlex.

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  9. Review
  10. Multifaceted roles of SUMO in DNA metabolism.Nucleus (Austin, Tex.) · 2024
    Review
  11. Article
  12. Review
  13. Article
  14. SUMO and the DNA damage response.Biochemical Society transactions · 2024
    Review
  15. Article
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  17. Article
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36 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

11 authors at 4 institutions in 3 countries.

Jean-Hugues GuervillyCentre National de la Recherche Scientifique, Unité Mixte de Recherche 7258, Inserm-Unité 1068, Centre de Recherche en Cancérologie de Marseille, Institut Paoli-Calmettes, F-13009 Marseille, France; Aix-Marseille Université, F-13284 Marseille, France. Electronic address: jean-hugues.guervilly@inserm.fr.
Arato TakedachiCentre National de la Recherche Scientifique, Unité Mixte de Recherche 7258, Inserm-Unité 1068, Centre de Recherche en Cancérologie de Marseille, Institut Paoli-Calmettes, F-13009 Marseille, France; Aix-Marseille Université, F-13284 Marseille, France.
Valeria NaimUniversité Paris-Sud, UMR 8200 CNRS, Equipe Labélisée La Ligue Contre le Cancer, Institut Gustave Roussy, 114 rue Edouard Vaillant, 94805 Villejuif Cedex, France.
Sarah ScaglioneCentre National de la Recherche Scientifique, Unité Mixte de Recherche 7258, Inserm-Unité 1068, Centre de Recherche en Cancérologie de Marseille, Institut Paoli-Calmettes, F-13009 Marseille, France; Aix-Marseille Université, F-13284 Marseille, France.
Charly ChawhanGenome Damage and Stability Centre, University of Sussex, Brighton BN1 9RQ, UK.
Yoann LoveraCentre National de la Recherche Scientifique, Unité Mixte de Recherche 7258, Inserm-Unité 1068, Centre de Recherche en Cancérologie de Marseille, Institut Paoli-Calmettes, F-13009 Marseille, France; Aix-Marseille Université, F-13284 Marseille, France.
Emmanuelle DesprasUniversité Paris-Sud, UMR 8200 CNRS, Equipe Labélisée La Ligue Contre le Cancer, Institut Gustave Roussy, 114 rue Edouard Vaillant, 94805 Villejuif Cedex, France.
Isao KuraokaDepartment of Chemistry, Graduate School of Engineering Science, Osaka University, 1-3 Machikaneyama, Toyonaka, Osaka 560-8531, Japan.
Patricia KannoucheUniversité Paris-Sud, UMR 8200 CNRS, Equipe Labélisée La Ligue Contre le Cancer, Institut Gustave Roussy, 114 rue Edouard Vaillant, 94805 Villejuif Cedex, France.
Filippo RosselliUniversité Paris-Sud, UMR 8200 CNRS, Equipe Labélisée La Ligue Contre le Cancer, Institut Gustave Roussy, 114 rue Edouard Vaillant, 94805 Villejuif Cedex, France.
Pierre-Henri L GaillardCentre National de la Recherche Scientifique, Unité Mixte de Recherche 7258, Inserm-Unité 1068, Centre de Recherche en Cancérologie de Marseille, Institut Paoli-Calmettes, F-13009 Marseille, France; Aix-Marseille Université, F-13284 Marseille, France. Electronic address: pierre-henri.gaillard@inserm.fr.
Centre National de la Recherche Scientifique · FRUniversité Paris-Sud · FRThe University of Osaka · JPUniversity of Sussex · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The SLX4 Fanconi anemia protein is a tumor suppressor that may act as a key regulator that engages the cell into specific genome maintenance pathways. Here, we show that the SLX4 complex is a SUMO E3 ligase that SUMOylates SLX4 itself and the XPF subunit of the DNA repair/recombination XPF-ERCC1 endonuclease. This SLX4-dependent activity is mediated by a remarkably specific interaction between SLX4 and the SUMO-charged E2 conjugating enzyme UBC9 and relies not only on newly identified SUMO-interacting motifs (SIMs) in SLX4 but also on its BTB domain. In contrast to its ubiquitin-binding UBZ4 motifs, SLX4 SIMs are dispensable for its DNA interstrand crosslink repair functions. Instead, while detrimental in response to global replication stress, the SUMO E3 ligase activity of the SLX4 complex is critical to prevent mitotic catastrophe following common fragile site expression.

Indexed as

DNA RepairGenomeAmino Acid SequenceCell Line, TumorDNA-Binding ProteinsDNA ReplicationGene Expression RegulationGenomic InstabilityHumansMolecular Sequence DataProtein BindingProtein Interaction Domains and MotifsProtein SubunitsRecombinant Fusion ProteinsRecombinasesSequence AlignmentDNA-Binding ProteinsProtein SubunitsRecombinant Fusion ProteinsRecombinasesSLX4 protein, humanSmall Ubiquitin-Related Modifier ProteinsUbiquitin-Conjugating EnzymesUbiquitin-Conjugating Enzyme UBC9Ubiquitin-Protein Ligasesxeroderma pigmentosum group F protein

Identifiers

PMID25533188
OpenAlexW2014017809

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.