Evidence map›Paper›PMID 36342193›Full record

ArticleGenetics2023

The Polo kinase Cdc5 is regulated at multiple levels in the adaptation response to telomere dysfunction.

Héloïse Coutelier, Oana Ilioaia, Jeanne Le Peillet, Marion Hamon, Damien D'Amours, Maria Teresa Teixeira, Zhou Xu

Open access · hybridAbstract read
In one paragraph

Article in Genetics, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.3field-weighted citation impact, top 47% 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

2 citing papers in PubMed, 3 citations in OpenAlex.

  1. Article
  2. DNA damage checkpoint execution and the rules of its disengagement.Frontiers in cell and developmental biology · 2022
    Review
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

7 authors at 3 institutions in 2 countries.

Héloïse CoutelierSorbonne Université, PSL, CNRS, UMR8226, Institut de Biologie Physico-Chimique, Laboratoire de Biologie Moléculaire et Cellulaire des Eucaryotes, 75005 Paris, France.
Oana IlioaiaSorbonne Université, CNRS, UMR7238, Institut de Biologie Paris-Seine, Laboratory of Computational and Quantitative Biology, 75005 Paris, France.
Jeanne Le PeilletSorbonne Université, CNRS, UMR7238, Institut de Biologie Paris-Seine, Laboratory of Computational and Quantitative Biology, 75005 Paris, France.
Marion HamonSorbonne Université, PSL, CNRS, FR550, Institut de Biologie Physico-Chimique, 75005 Paris, France.
Damien D'AmoursOttawa Institute of Systems Biology, Department of Cellular and Molecular Medicine, University of Ottawa, Ottawa, ON K1H 8M5, Canada.
Maria Teresa TeixeiraSorbonne Université, PSL, CNRS, UMR8226, Institut de Biologie Physico-Chimique, Laboratoire de Biologie Moléculaire et Cellulaire des Eucaryotes, 75005 Paris, France.ORCID 0000-0002-9466-7951
Zhou XuSorbonne Université, CNRS, UMR7238, Institut de Biologie Paris-Seine, Laboratory of Computational and Quantitative Biology, 75005 Paris, France.ORCID 0000-0001-9468-1406
Centre National de la Recherche Scientifique · FRUniversité Claude Bernard Lyon 1 · FRUniversity of Ottawa · CA

Funding

CIHR FDN-167265
6 · The paper itself

Abstract

Telomere dysfunction activates the DNA damage checkpoint to induce a cell cycle arrest. After an extended period of time, however, cells can bypass the arrest and undergo cell division despite the persistence of the initial damage, a process called adaptation to DNA damage. The Polo kinase Cdc5 in Saccharomyces cerevisiae is essential for adaptation and for many other cell cycle processes. How the regulation of Cdc5 in response to telomere dysfunction relates to adaptation is not clear. Here, we report that Cdc5 protein level decreases after telomere dysfunction in a Mec1-, Rad53- and Ndd1-dependent manner. This regulation of Cdc5 is important to maintain long-term cell cycle arrest but not for the initial checkpoint arrest. We find that both Cdc5 and the adaptation-deficient mutant protein Cdc5-ad are heavily phosphorylated and several phosphorylation sites modulate adaptation efficiency. The PP2A phosphatases are involved in Cdc5-ad phosphorylation status and contribute to adaptation mechanisms. We finally propose that Cdc5 orchestrates multiple cell cycle pathways to promote adaptation.

Indexed as

Protein Serine-Threonine KinasesSaccharomyces cerevisiae ProteinsCell Cycle ProteinsCheckpoint Kinase 2DNA DamagePhosphorylationProtein KinasesSaccharomyces cerevisiaeTelomereCDC5 protein, S cerevisiaeCell Cycle ProteinsCheckpoint Kinase 2Protein KinasesProtein Serine-Threonine KinasesSaccharomyces cerevisiae Proteinsadaptation to DNA damageDNA damage checkpointPolo kinase Cdc5PP2Atelomere

Identifiers

PMID36342193
PMCPMC9836022
OpenAlexW4308365290

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.