Evidence map›Paper›PMID 27831827›Full record

ArticleCell cycle (Georgetown, Tex.)2016

Mitotic entry: The interplay between Cdk1, Plk1 and Bora.

Alfonso Parrilla, Luca Cirillo, Yann Thomas, Monica Gotta, Lionel Pintard, Anna Santamaria

Open access · bronzeAbstract read
In one paragraph

Article in Cell cycle (Georgetown, Tex.), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.3field-weighted citation impact, top 13% 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

27 citing papers in PubMed, 47 citations in OpenAlex.

  1. Trial
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  8. Only InfantInternational journal of molecular sciences · 2024
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  9. Review
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  12. DNA damage checkpoint execution and the rules of its disengagement.Frontiers in cell and developmental biology · 2022
    Review
  13. Article
  14. Article
  15. Design of new disubstituted imidazo[1,2-Journal of enzyme inhibition and medicinal chemistry · 2020
    Article
  16. Article
  17. Article
  18. Cancers · 2020
    Article
  19. Article
  20. Article
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 4 institutions in 3 countries.

Alfonso Parrillaa Cell Cycle and Cancer Laboratory, Biomedical Research Group in Gynecology, Vall Hebron Research Institute (VHIR) - Universitat Autònoma de Barcelona (UAB) , Barcelona , Spain.
Luca Cirillob Department of Cell Physiology and Metabolism , Faculty of Medicine, University of Geneva , Geneva , Switzerland.
Yann Thomasc Jacques Monod Institute, UMR7592, Paris-Diderot University, Centre National de la Recherche Scientifique , Paris , France.
Monica Gottab Department of Cell Physiology and Metabolism , Faculty of Medicine, University of Geneva , Geneva , Switzerland.
Lionel Pintardc Jacques Monod Institute, UMR7592, Paris-Diderot University, Centre National de la Recherche Scientifique , Paris , France.
Anna Santamariaa Cell Cycle and Cancer Laboratory, Biomedical Research Group in Gynecology, Vall Hebron Research Institute (VHIR) - Universitat Autònoma de Barcelona (UAB) , Barcelona , Spain.
Universitat Autònoma de Barcelona · ESUniversity of Geneva · CHInstitut Jacques Monod · FRUniversité Paris Cité · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Polo-like kinase 1 (Plk1) is an important mitotic kinase that is crucial for entry into mitosis after recovery from DNA damage-induced cell cycle arrest. Plk1 activation is promoted by the conserved protein Bora (SPAT-1 in C. elegans), which stimulates the phosphorylation of a conserved residue in the activation loop by the Aurora A kinase. In a recent article published in Cell Reports, we show that the master mitotic kinase Cdk1 contributes to Plk1 activation through SPAT-1/Bora phosphorylation. We identified 3 conserved Sp/Tp residues that are located in the N-terminal, most conserved part, of SPAT-1/Bora. Phosphorylation of these sites by Cdk1 is essential for Plk1 function in mitotic entry in C. elegans embryos and during DNA damage checkpoint recovery in mammalian cells. Here, using an untargeted Förster Resonance Energy Transfer (FRET) biosensor to monitor Plk1 activation, we provide additional experimental evidence supporting the importance of these phosphorylation sites for Plk1 activation and subsequent mitotic entry after DNA damage. We also briefly discuss the mechanism of Plk1 activation and the potential role of Bora phosphorylation by Cdk1 in this process. As Plk1 is overexpressed in cancer cells and this correlates with poor prognosis, understanding how Bora contributes to Plk1 activation is paramount for the development of innovative therapeutical approaches.

Indexed as

MitosisCDC2 Protein KinaseCell Cycle CheckpointsCell Cycle ProteinsEnzyme ActivationFluorescence Resonance Energy TransferHeLa CellsHumansPhosphorylationPolo-Like Kinase 1Protein Serine-Threonine KinasesProto-Oncogene Proteinsbora protein, humanCDC2 Protein KinaseCell Cycle ProteinsPolo-Like Kinase 1Protein Serine-Threonine KinasesProto-Oncogene ProteinsBoraCdk1FRETPlk1 activation

Identifiers

PMID27831827
PMCPMC5176151
OpenAlexW2551169910

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.