Evidence map›Paper›PMID 20053638›Full record

ArticleJournal of cell science2010

Cdc20 is required for the post-anaphase, KEN-dependent degradation of centromere protein F.

Mark D J Gurden, Andrew J Holland, Wouter van Zon, Anthony Tighe, Mailys A Vergnolle, Douglas A Andres, H Peter Spielmann, Marcos Malumbres, Rob M F Wolthuis, Don W Cleveland and 1 more

Open access · greenAbstract read
In one paragraph

Article in Journal of cell science, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

38 citing papers in PubMed, 56 citations in OpenAlex.

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  19. Taming the Beast: Control of APC/CCold Spring Harbor symposia on quantitative biology · 2017
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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 4 countries.

Mark D J GurdenFaculty of Life Sciences, Michael Smith Building, University of Manchester, Manchester M13 9PT, UK.
Andrew J Holland
Wouter van Zon
Anthony Tighe
Mailys A Vergnolle
Douglas A Andres
H Peter Spielmann
Marcos Malumbres
Rob M F Wolthuis
Don W Cleveland
Stephen S Taylor
University of Manchester · GBLudwig Cancer Research · USThe Netherlands Cancer Institute · NLUniversity of Kentucky · USSpanish National Cancer Research Centre · ES

Funding

Biotechnology and Biological Sciences Research Council BB/E015034/1Cancer Research UK 11913Wellcome Trust
6 · The paper itself

Abstract

Progression through mitosis and cytokinesis requires the sequential proteolysis of several cell-cycle regulators. This proteolysis is mediated by the ubiquitin-proteasome system, with the E3 ligase being the anaphase-promoting complex, also known as the cyclosome (APC/C). The APC/C is regulated by two activators, namely Cdc20 and Cdh1. The current view is that prior to anaphase, the APC/C is activated by Cdc20, but that following anaphase, APC/C switches to Cdh1-dependent activation. However, here we present an analysis of the kinetochore protein Cenp-F that is inconsistent with this notion. Although it has long been appreciated that Cenp-F is degraded sometime during or after mitosis, exactly when and how has not been clear. Here we show that degradation of Cenp-F initiates about six minutes after anaphase, and that this is dependent on a C-terminal KEN-box. Although these two observations are consistent with Cenp-F being a substrate of Cdh1-activated APC/C, Cenp-F is degraded normally in Cdh1-null cells. By contrast, RNAi-mediated repression of APC/C subunits or Cdc20 does inhibit Cenp-F degradation. These findings therefore suggest that the APC/C does not simply 'switch' upon anaphase onset; rather, our observations indicate that Cdc20 also contributes to post-anaphase activation of the APC/C. We also show that the post-anaphase, KEN-box-dependent degradation of Cenp-F requires it to be farnesylated, a post-translational modification usually linked to membrane association. Because so many of the behaviours of Cenp-F are farnesylation-dependent, we suggest that this modification plays a more global role in Cenp-F function.

Indexed as

Anaphase-Promoting Complex-CyclosomeAnimalsAntigens, CDCadherinsCdc20 ProteinsCdh1 ProteinsCell Cycle ProteinsCell Line, TumorCells, CulturedChromosomal Proteins, Non-HistoneHumansKinetochoresMiceMicrofilament ProteinsMicroscopyPrenylationAnaphase-Promoting Complex-CyclosomeAntigens, CDCadherinsCDC20 protein, humanCdc20 protein, mouseCdc20 ProteinsCDH1 protein, humanCdh1 ProteinsCell Cycle Proteinscentromere protein Ecentromere protein FChromosomal Proteins, Non-HistoneFzr1 protein, mouseMicrofilament ProteinsUbiquitin-Protein Ligase Complexes

Identifiers

PMID20053638
PMCPMC2816182
OpenAlexW2163081961

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.