Evidence map›Paper›PMID 38321267›Full record

ArticleThe EMBO journal2024

Qualitative rather than quantitative phosphoregulation shapes the end of meiosis I in budding yeast.

Dunja Celebic, Irem Polat, Véronique Legros, Guillaume Chevreux, Katja Wassmann, Sandra A Touati

Open access · diamondAbstract read
In one paragraph

Article in The EMBO journal, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
2.1field-weighted citation impact, top 14% 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

3 citing papers in PubMed, 9 citations in OpenAlex.

  1. 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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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

6 authors at 1 institution in 1 country.

Dunja CelebicUniversité Paris Cité, CNRS, Institut Jacques Monod, 75013, Paris, France.
Irem PolatUniversité Paris Cité, CNRS, Institut Jacques Monod, 75013, Paris, France.
Véronique LegrosUniversité Paris Cité, CNRS, Institut Jacques Monod, 75013, Paris, France.ORCID http://orcid.org/0000-0002-2502-2914
Guillaume ChevreuxUniversité Paris Cité, CNRS, Institut Jacques Monod, 75013, Paris, France.
Katja WassmannUniversité Paris Cité, CNRS, Institut Jacques Monod, 75013, Paris, France.ORCID http://orcid.org/0000-0001-5442-5192
Sandra A TouatiUniversité Paris Cité, CNRS, Institut Jacques Monod, 75013, Paris, France. sandra.touati@ijm.fr.ORCID http://orcid.org/0000-0002-0007-2130
Centre National de la Recherche Scientifique · FR

Funding

Agence Nationale de la Recherche (ANR) ANR-21-CE13-0026Fondation ARC pour la Recherche sur le Cancer (ARC) ARCPJA12020060002043Sorbonne Université (Sorbonne University) Tremplin Sorbonne Université 2020
6 · The paper itself

Abstract

Exit from mitosis is brought about by dramatic changes in the phosphoproteome landscape. A drop in Cyclin-dependent kinase (Cdk) activity, the master regulatory kinase, and activation of counteracting phosphatases such as Cdc14 in budding yeast, results in ordered substrate dephosphorylation, allowing entry into a new cell cycle and replication licensing. In meiosis however, two cell divisions have to be executed without intermediate DNA replication, implying that global phosphorylation and dephosphorylation have to be adapted to the challenges of meiosis. Using a global time-resolved phosphoproteomics approach in budding yeast, we compared the phosphoproteome landscape between mitotic exit and the transition from meiosis I to meiosis II. We found that unlike exit from mitosis, Cdk phosphomotifs remain mostly stably phosphorylated at the end of meiosis I, whereas a majority of Cdk-unrelated motifs are reset by dephosphorylation. However, inducing an artificial drop of Cdk at metaphase of meiosis I leads to ordered substrate dephosphorylation, comparable to mitosis, indicating that phosphoregulation of substrates at the end of meiosis I is thus mainly qualitatively rather than quantitatively ordered.

Indexed as

Saccharomyces cerevisiae ProteinsSaccharomycetalesCell Cycle ProteinsMeiosisMitosisPhosphorylationProtein Tyrosine PhosphatasesCell Cycle ProteinsProtein Tyrosine PhosphatasesSaccharomyces cerevisiae ProteinsCdkCell CycleMeiosisMetaphase I to Anaphase I Transition

Identifiers

PMID38321267
PMCPMC10987528
OpenAlexW4391576129

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.