Evidence map›Paper›PMID 24391510›Full record

ArticlePLoS genetics2014

PP2A/B55 and Fcp1 regulate Greatwall and Ensa dephosphorylation during mitotic exit.

Nadia Hégarat, Clare Vesely, P K Vinod, Cory Ocasio, Nisha Peter, Julian Gannon, Antony W Oliver, Béla Novák, Helfrid Hochegger

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in PLoS genetics, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
4.4field-weighted citation impact, top 5% 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

39 citing papers in PubMed, 64 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Cell cycle control during early embryogenesis.Development (Cambridge, England) · 2021
    Article
  7. Article
  8. Article
  9. Biology open · 2021
    Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Protein phosphatases in the regulation of mitosis.The Journal of cell biology · 2019
    Review
  20. Article
4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

9 authors at 3 institutions in 1 country.

Nadia HégaratGenome Damage and Stability Centre, School of Life Sciences, University of Sussex, Falmer, Brighton, United Kingdom.
Clare VeselyGenome Damage and Stability Centre, School of Life Sciences, University of Sussex, Falmer, Brighton, United Kingdom.
P K VinodOxford Centre for Integrative Systems Biology, Department of Biochemistry, University of Oxford, Oxford, United Kingdom.
Cory OcasioGenome Damage and Stability Centre, School of Life Sciences, University of Sussex, Falmer, Brighton, United Kingdom.
Nisha PeterGenome Damage and Stability Centre, School of Life Sciences, University of Sussex, Falmer, Brighton, United Kingdom.
Julian GannonGenome Stability, Cancer Research UK, Clare Hall Laboratories, South Mimms, Herts, United Kingdom.
Antony W OliverGenome Damage and Stability Centre, School of Life Sciences, University of Sussex, Falmer, Brighton, United Kingdom.
Béla NovákOxford Centre for Integrative Systems Biology, Department of Biochemistry, University of Oxford, Oxford, United Kingdom.
Helfrid HocheggerGenome Damage and Stability Centre, School of Life Sciences, University of Sussex, Falmer, Brighton, United Kingdom.
University of Sussex · GBUniversity of Oxford · GBCancer Research UK · GB

Funding

Cancer Research UK 14532Cancer Research UK C28206/A14499
6 · The paper itself

Abstract

Entry into mitosis is triggered by activation of Cdk1 and inactivation of its counteracting phosphatase PP2A/B55. Greatwall kinase inactivates PP2A/B55 via its substrates Ensa and ARPP19. Both Greatwall and Ensa/ARPP19 are regulated by phosphorylation, but the dynamic regulation of Greatwall activity and the phosphatases that control Greatwall kinase and its substrates are poorly understood. To address these questions we applied a combination of mathematical modelling and experiments using phospho-specific antibodies to monitor Greatwall, Ensa/ARPP19 and Cdk substrate phosphorylation during mitotic entry and exit. We demonstrate that PP2A/B55 is required for Gwl dephosphorylation at the essential Cdk site Thr194. Ensa/ARPP19 dephosphorylation is mediated by the RNA Polymerase II carboxy terminal domain phosphatase Fcp1. Surprisingly, inhibition or depletion of neither Fcp1 nor PP2A appears to block dephosphorylation of the bulk of mitotic Cdk1 substrates during mitotic exit. Taken together our results suggest a hierarchy of phosphatases coordinating Greatwall, Ensa/ARPP19 and Cdk substrate dephosphorylation during mitotic exit.

Indexed as

CDC2 Protein KinaseCell CycleCyclin BGene Regulatory NetworksHeLa CellsHumansMicrotubule-Associated ProteinsMitosisPhosphoprotein PhosphatasesPhosphoproteinsPhosphorylationProtein Phosphatase 2Protein Serine-Threonine KinasesCDC2 Protein Kinasecyclic AMP-regulated phosphoprotein 19Cyclin BFcp1 protein, humanMASTL protein, humanMicrotubule-Associated ProteinsPhosphoprotein PhosphatasesPhosphoproteinsProtein Phosphatase 2Protein Serine-Threonine Kinases

Identifiers

PMID24391510
PMCPMC3879168
OpenAlexW2053395877

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.