Evidence map›Paper›PMID 32307883›Full record

ArticleEMBO reports2020

A unique binding mode of Nek2A to the APC/C allows its ubiquitination during prometaphase.

Claudio Alfieri, Thomas Tischer, David Barford

Abstract read
In one paragraph

Article in EMBO reports, 2020. 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
–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

19 citing papers in PubMed.

  1. Article
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  3. Article
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  5. Article
  6. Cryo-EM structures of apo-APC/C and APC/CNature communications · 2024
    Article
  7. Article
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  11. Review
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  16. Review
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors.

Claudio AlfieriMRC Laboratory of Molecular Biology, Cambridge, UK.ORCID 0000-0003-3215-1607
Thomas TischerMRC Laboratory of Molecular Biology, Cambridge, UK.ORCID 0000-0002-6845-2762
David BarfordMRC Laboratory of Molecular Biology, Cambridge, UK.ORCID 0000-0001-8810-950X

Funding

Cancer Research UK 14109Cancer Research UK 24307Medical Research Council MC_UP_1201/6
6 · The paper itself

Abstract

The anaphase-promoting complex (APC/C) is the key E3 ubiquitin ligase which directs mitotic progression and exit by catalysing the sequential ubiquitination of specific substrates. The activity of the APC/C in mitosis is restrained by the spindle assembly checkpoint (SAC), which coordinates chromosome segregation with the assembly of the mitotic spindle. The SAC effector is the mitotic checkpoint complex (MCC), which binds and inhibits the APC/C. It is incompletely understood how the APC/C switches substrate specificity in a cell cycle-specific manner. For instance, it is unclear how in prometaphase, when APC/C activity towards cyclin B and securin is repressed by the MCC, the kinase Nek2A is ubiquitinated. Here, we combine biochemical and structural analysis with functional studies in cells to show that Nek2A is a conformational-specific binder of the APC/C-MCC complex (APC/C

Indexed as

M Phase Cell Cycle CheckpointsPrometaphaseAnaphase-Promoting Complex-CyclosomeCdc20 ProteinsCell Cycle ProteinsHeLa CellsHumansMitosisSpindle ApparatusUbiquitinationAnaphase-Promoting Complex-CyclosomeCdc20 ProteinsCell Cycle Proteinsanaphase-promoting complexcell cyclecryo-EME3 ligasespindle assembly checkpoint

Identifiers

PMID32307883
PMCPMC7271329

What OpenQuestion holds

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Registered trials

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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.