Evidence map›Paper›PMID 25144743›Full record

ArticlePloS one2014

Structural and biochemical characterization of the Cop9 signalosome CSN5/CSN6 heterodimer.

Melissa Birol, Radoslav Ivanov Enchev, André Padilla, Florian Stengel, Ruedi Aebersold, Stéphane Betzi, Yinshan Yang, François Hoh, Matthias Peter, Christian Dumas and 1 more

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.1field-weighted citation impact, top 12% 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

19 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
  2. COP9 Signalosome's Role in Plant Defense Mechanisms.Plants (Basel, Switzerland) · 2025
    Review
  3. Article
  4. Review
  5. Computational exploration of the significance ofWorld journal of clinical oncology · 2023
    Article
  6. Article
  7. Structural dynamics of the human COP9 signalosome revealed by cross-linking mass spectrometry and integrative modeling.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Review
  16. Article
  17. Article
  18. Protein neddylation: beyond cullin-RING ligases.Nature reviews. Molecular cell biology · 2015
    Review
  19. 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

11 authors at 5 institutions in 2 countries.

Melissa BirolCentre de Biochimie Structurale, Unité Mixte de Recherche (UMR) 5048, Centre National de Recherche Scientifique (CNRS), Université Montpellier 1 (UM1), Université Montpellier 2 (UM2), Montpellier, France; Institut national de la santé et de la recherche médicale (INSERM) U1054, Paris, France.
Radoslav Ivanov EnchevETH Zurich, Department of Biology, Institute of Biochemistry, Zurich, Switzerland.
André PadillaCentre de Biochimie Structurale, Unité Mixte de Recherche (UMR) 5048, Centre National de Recherche Scientifique (CNRS), Université Montpellier 1 (UM1), Université Montpellier 2 (UM2), Montpellier, France; Institut national de la santé et de la recherche médicale (INSERM) U1054, Paris, France.
Florian StengelETH Zurich, Department of Biology, Institute of Molecular Systems Biology, Zurich, Switzerland.
Ruedi AebersoldETH Zurich, Department of Biology, Institute of Molecular Systems Biology, Zurich, Switzerland; Faculty of Science, University of Zurich, Zurich, Switzerland.
Stéphane BetziCentre de Recherche en Cancérologie de Marseille, Centre de Biochimie Structurale, Unité Mixte de Recherche (UMR) 7258, Institut national de la santé et de la recherche médicale (INSERM) U1068, Institut Paoli-Calmettes, Aix-Marseille Université UM105, Marseille, France.
Yinshan YangCentre de Biochimie Structurale, Unité Mixte de Recherche (UMR) 5048, Centre National de Recherche Scientifique (CNRS), Université Montpellier 1 (UM1), Université Montpellier 2 (UM2), Montpellier, France; Institut national de la santé et de la recherche médicale (INSERM) U1054, Paris, France.
François HohCentre de Biochimie Structurale, Unité Mixte de Recherche (UMR) 5048, Centre National de Recherche Scientifique (CNRS), Université Montpellier 1 (UM1), Université Montpellier 2 (UM2), Montpellier, France; Institut national de la santé et de la recherche médicale (INSERM) U1054, Paris, France.
Matthias PeterETH Zurich, Department of Biology, Institute of Biochemistry, Zurich, Switzerland.
Christian DumasCentre de Biochimie Structurale, Unité Mixte de Recherche (UMR) 5048, Centre National de Recherche Scientifique (CNRS), Université Montpellier 1 (UM1), Université Montpellier 2 (UM2), Montpellier, France; Institut national de la santé et de la recherche médicale (INSERM) U1054, Paris, France.
Aude EchalierCentre de Biochimie Structurale, Unité Mixte de Recherche (UMR) 5048, Centre National de Recherche Scientifique (CNRS), Université Montpellier 1 (UM1), Université Montpellier 2 (UM2), Montpellier, France; Institut national de la santé et de la recherche médicale (INSERM) U1054, Paris, France.
ETH Zurich · CHInserm · FRCentre de Biologie Structurale · FRCentre National de la Recherche Scientifique · FRUniversité de Montpellier · FR

Funding

Wellcome TrustWellcome Trust 095951
6 · The paper itself

Abstract

The Cop9 signalosome complex (CSN) regulates the functional cycle of the major E3 ubiquitin ligase family, the cullin RING E3 ubiquitin ligases (CRLs). Activated CRLs are covalently modified by the ubiquitin-like protein Nedd8 (neural precursor cell expressed developmentally down-regulated protein 8). CSN serves an essential role in myriad cellular processes by reversing this modification through the isopeptidase activity of its CSN5 subunit. CSN5 alone is inactive due to an auto-inhibited conformation of its catalytic domain. Here we report the molecular basis of CSN5 catalytic domain activation and unravel a molecular hierarchy in CSN deneddylation activity. The association of CSN5 and CSN6 MPN (for Mpr1/Pad1 N-terminal) domains activates its isopeptidase activity. The CSN5/CSN6 module, however, is inefficient in CRL deneddylation, indicating a requirement of further elements in this reaction such as other CSN subunits. A hybrid molecular model of CSN5/CSN6 provides a structural framework to explain these functional observations. Docking this model into a published CSN electron density map and using distance constraints obtained from cross-linking coupled to mass-spectrometry, we find that the C-termini of the CSN subunits could form a helical bundle in the centre of the structure. They likely play a key scaffolding role in the spatial organization of CSN and precise positioning of the dimeric MPN catalytic core.

Indexed as

Protein MultimerizationAdaptor Proteins, Signal TransducingCOP9 Signalosome ComplexHumansIntracellular Signaling Peptides and ProteinsModels, MolecularMultiprotein ComplexesNEDD8 ProteinPeptide HydrolasesProtein BindingProtein ConformationProtein Interaction Domains and MotifsProtein SubunitsUbiquitinsAdaptor Proteins, Signal TransducingCOP9 Signalosome ComplexCOPS5 protein, humanCOPS6 protein, humanIntracellular Signaling Peptides and ProteinsMultiprotein ComplexesNEDD8 ProteinNEDD8 protein, humanPeptide HydrolasesProtein SubunitsUbiquitins

Identifiers

PMID25144743
PMCPMC4140821
OpenAlexW2170634643

What OpenQuestion holds

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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.