Evidence map›Paper›PMID 25043029›Full record

ArticleNature2014

Molecular architecture and mechanism of the anaphase-promoting complex.

Lei-Fu Chang, Ziguo Zhang, Jing Yang, Stephen H McLaughlin, David Barford

Open access · greenAbstract read
In one paragraph

Article in Nature, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 142 papers.

0numbers the graph read from it
0cells of the map it votes in
142citing papers in PubMed
12.2field-weighted citation impact, top 1% 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

142 citing papers in PubMed, 209 citations in OpenAlex.

  1. Article
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  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Cryo-EM structures of apo-APC/C and APC/CNature communications · 2024
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. The Anaphase-Promoting Complex/Cyclosome Is a Cellular Ageing Regulator.International journal of molecular sciences · 2022
    Review

82 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

5 authors at 2 institutions in 1 country.

Lei-Fu Chang *Division of Structural Biology, Institute of Cancer Research, 237 Fulham Road, London, SW3 6JB, UK.
Ziguo Zhang *Division of Structural Biology, Institute of Cancer Research, 237 Fulham Road, London, SW3 6JB, UK.
Jing YangDivision of Structural Biology, Institute of Cancer Research, 237 Fulham Road, London, SW3 6JB, UK.
Stephen H McLaughlinMRC Laboratory of Molecular Biology, Cambridge, CB2 0QH, UK.
David BarfordDivision of Structural Biology, Institute of Cancer Research, 237 Fulham Road, London, SW3 6JB, UK.
MRC Laboratory of Molecular Biology · GBInstitute of Cancer Research · GB

Funding

Cancer Research UK 14109Medical Research Council MC_UP_1201/6
6 · The paper itself

Abstract

The ubiquitination of cell cycle regulatory proteins by the anaphase-promoting complex/cyclosome (APC/C) controls sister chromatid segregation, cytokinesis and the establishment of the G1 phase of the cell cycle. The APC/C is an unusually large multimeric cullin-RING ligase. Its activity is strictly dependent on regulatory coactivator subunits that promote APC/C-substrate interactions and stimulate its catalytic reaction. Because the structures of many APC/C subunits and their organization within the assembly are unknown, the molecular basis for these processes is poorly understood. Here, from a cryo-electron microscopy reconstruction of a human APC/C-coactivator-substrate complex at 7.4 Å resolution, we have determined the complete secondary structural architecture of the complex. With this information we identified protein folds for structurally uncharacterized subunits, and the definitive location of all 20 APC/C subunits within the 1.2 MDa assembly. Comparison with apo APC/C shows that the coactivator promotes a profound allosteric transition involving displacement of the cullin-RING catalytic subunits relative to the degron-recognition module of coactivator and APC10. This transition is accompanied by increased flexibility of the cullin-RING subunits and enhanced affinity for UBCH10-ubiquitin, changes which may contribute to coactivator-mediated stimulation of APC/C E3 ligase activity.

Indexed as

Allosteric RegulationAnaphase-Promoting Complex-CyclosomeApc10 Subunit, Anaphase-Promoting Complex-CyclosomeCatalytic DomainCdh1 ProteinsCryoelectron MicroscopyHumansModels, MolecularPliabilityProtein FoldingProtein Structure, SecondaryProtein SubunitsUbiquitinUbiquitinationUbiquitin-Conjugating EnzymesANAPC10 protein, humanAnaphase-Promoting Complex-CyclosomeApc10 Subunit, Anaphase-Promoting Complex-CyclosomeCdh1 ProteinsProtein SubunitsUBE2C protein, humanUbiquitinUbiquitin-Conjugating Enzymes

Identifiers

PMID25043029
PMCPMC4456660
OpenAlexW2098964644

What OpenQuestion holds

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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.