Evidence map›Paper›PMID 25487150›Full record

ArticleNature2015

A PP1-PP2A phosphatase relay controls mitotic progression.

Agnes Grallert, Elvan Boke, Anja Hagting, Ben Hodgson, Yvonne Connolly, John R Griffiths, Duncan L Smith, Jonathon Pines, Iain M Hagan

Erratum issuedOpen access · greenAbstract read
In one paragraph

Article in Nature, 2015. 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 117 papers.

0numbers the graph read from it
0cells of the map it votes in
117citing papers in PubMed
9.3field-weighted citation impact, top 1% 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

117 citing papers in PubMed, 195 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. 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
  17. Review
  18. Article
  19. Review
  20. Review

57 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors at 1 institution in 1 country.

Agnes Grallert *Cell Division Group, CRUK Manchester Institute, University of Manchester, Wilmslow Road, Manchester, M20 4BX, UK.
Elvan Boke *Cell Division Group, CRUK Manchester Institute, University of Manchester, Wilmslow Road, Manchester, M20 4BX, UK.
Anja HagtingThe Gurdon Institute, University of Cambridge, Cambridge CB2 1QN, UK.
Ben HodgsonCell Division Group, CRUK Manchester Institute, University of Manchester, Wilmslow Road, Manchester, M20 4BX, UK.
Yvonne ConnollyBiological Mass Spectrometry, CRUK Manchester Institute, University of Manchester, Wilmslow Road, Manchester, M20 4BX, UK.
John R GriffithsBiological Mass Spectrometry, CRUK Manchester Institute, University of Manchester, Wilmslow Road, Manchester, M20 4BX, UK.
Duncan L SmithBiological Mass Spectrometry, CRUK Manchester Institute, University of Manchester, Wilmslow Road, Manchester, M20 4BX, UK.
Jonathon PinesThe Gurdon Institute, University of Cambridge, Cambridge CB2 1QN, UK.
Iain M HaganCell Division Group, CRUK Manchester Institute, University of Manchester, Wilmslow Road, Manchester, M20 4BX, UK.
University of Cambridge · GB

Funding

Cancer Research UK 13678Cancer Research UK 16406Cancer Research UK A13678Cancer Research UK A16406Cancer Research UK C147/A16406Cancer Research UK C29/A13678Wellcome Trust 092096
6 · The paper itself

Abstract

The widespread reorganization of cellular architecture in mitosis is achieved through extensive protein phosphorylation, driven by the coordinated activation of a mitotic kinase network and repression of counteracting phosphatases. Phosphatase activity must subsequently be restored to promote mitotic exit. Although Cdc14 phosphatase drives this reversal in budding yeast, protein phosphatase 1 (PP1) and protein phosphatase 2A (PP2A) activities have each been independently linked to mitotic exit control in other eukaryotes. Here we describe a mitotic phosphatase relay in which PP1 reactivation is required for the reactivation of both PP2A-B55 and PP2A-B56 to coordinate mitotic progression and exit in fission yeast. The staged recruitment of PP1 (the Dis2 isoform) to the regulatory subunits of the PP2A-B55 and PP2A-B56 (B55 also known as Pab1; B56 also known as Par1) holoenzymes sequentially activates each phosphatase. The pathway is blocked in early mitosis because the Cdk1-cyclin B kinase (Cdk1 also known as Cdc2) inhibits PP1 activity, but declining cyclin B levels later in mitosis permit PP1 to auto-reactivate. PP1 first reactivates PP2A-B55; this enables PP2A-B55 in turn to promote the reactivation of PP2A-B56 by dephosphorylating a PP1-docking site in PP2A-B56, thereby promoting the recruitment of PP1. PP1 recruitment to human, mitotic PP2A-B56 holoenzymes and the sequences of these conserved PP1-docking motifs suggest that PP1 regulates PP2A-B55 and PP2A-B56 activities in a variety of signalling contexts throughout eukaryotes.

Indexed as

MitosisAmino Acid MotifsAmino Acid SequenceBinding SitesCDC2 Protein KinaseChromosome SegregationConserved SequenceCyclin BEnzyme ActivationHeLa CellsHoloenzymesHumansIsoenzymesMolecular Sequence DataPhosphorylationProtein Phosphatase 1CDC2 Protein KinaseCyclin BHoloenzymesIsoenzymesProtein Phosphatase 1Protein Phosphatase 2Protein SubunitsSchizosaccharomyces pombe Proteins

Identifiers

PMID25487150
PMCPMC4338534
OpenAlexW2054261736

What OpenQuestion holds

Textmetadata
LicenceTDM
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.