Evidence map›Paper›PMID 29650682›Full record

ArticleThe EMBO journal2018

Phosphoproteome dynamics during mitotic exit in budding yeast.

Sandra A Touati, Meghna Kataria, Andrew W Jones, Ambrosius P Snijders, Frank Uhlmann

Open access · hybridAbstract read
In one paragraph

Article in The EMBO journal, 2018. 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
2.8field-weighted citation impact, top 10% 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.

  1. Mitotic kinase regulation of DNA replication forks.bioRxiv : the preprint server for biology · 2026
    Article
  2. Article
  3. Decoding Cdk1 control: from mitotic thresholds to meiotic specificity.Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 2026
    Review
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  5. Article
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  8. Review
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  11. Septin Organization and Dynamics for Budding Yeast Cytokinesis.Journal of fungi (Basel, Switzerland) · 2024
    Review
  12. Article
  13. Article
  14. Article
  15. Analog-sensitive Cdk1 as a tool to study mitotic exit: protein phosphatase 1 is required downstream from Cdk1 inactivation in budding yeast.Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 2023
    Article
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Sandra A TouatiChromosome Segregation Laboratory, The Francis Crick Institute, London, UK.
Meghna KatariaChromosome Segregation Laboratory, The Francis Crick Institute, London, UK.
Andrew W JonesMass Spectrometry Proteomics Science Technology Platform, The Francis Crick Institute, London, UK.
Ambrosius P SnijdersMass Spectrometry Proteomics Science Technology Platform, The Francis Crick Institute, London, UK.
Frank UhlmannChromosome Segregation Laboratory, The Francis Crick Institute, London, UK frank.uhlmann@crick.ac.uk.ORCID 0000-0002-3527-6619
The Francis Crick Institute · GB

Funding

Cancer Research UK FC001198Medical Research Council FC001198Wellcome TrustWellcome Trust FC001198
6 · The paper itself

Abstract

The cell division cycle culminates in mitosis when two daughter cells are born. As cyclin-dependent kinase (Cdk) activity reaches its peak, the anaphase-promoting complex/cyclosome (APC/C) is activated to trigger sister chromatid separation and mitotic spindle elongation, followed by spindle disassembly and cytokinesis. Degradation of mitotic cyclins and activation of Cdk-counteracting phosphatases are thought to cause protein dephosphorylation to control these sequential events. Here, we use budding yeast to analyze phosphorylation dynamics of 3,456 phosphosites on 1,101 proteins with high temporal resolution as cells progress synchronously through mitosis. This reveals that successive inactivation of S and M phase Cdks and of the mitotic kinase Polo contributes to order these dephosphorylation events. Unexpectedly, we detect as many new phosphorylation events as there are dephosphorylation events. These correlate with late mitotic kinase activation and identify numerous candidate targets of these kinases. These findings revise our view of mitotic exit and portray it as a dynamic process in which a range of mitotic kinases contribute to order both protein dephosphorylation and phosphorylation.

Indexed as

Cell CycleCell Cycle ProteinsCytokinesisMitosisPhosphoprotein PhosphatasesPhosphoproteinsPhosphorylationProteolysisProteomeSaccharomyces cerevisiae ProteinsSaccharomycetalesCell Cycle ProteinsPhosphoprotein PhosphatasesPhosphoproteinsProteomeSaccharomyces cerevisiae Proteinscell cyclekinasesmitosisphosphatasesphosphoproteomics

Identifiers

PMID29650682
PMCPMC5978319
OpenAlexW2797111959

What OpenQuestion holds

Textmetadata
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.