Evidence map›Paper›PMID 19793917›Full record

ArticleMolecular biology of the cell2009

The M phase kinase Greatwall (Gwl) promotes inactivation of PP2A/B55delta, a phosphatase directed against CDK phosphosites.

Priscila V Castilho, Byron C Williams, Satoru Mochida, Yong Zhao, Michael L Goldberg

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 119 papers.

0numbers the graph read from it
0cells of the map it votes in
119citing papers in PubMed
7.7field-weighted citation impact, top 2% 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

119 citing papers in PubMed, 190 citations in OpenAlex.

  1. Article
  2. Article
  3. Egg Overactivation-An Overlooked Phenomenon of Gamete Physiology.International journal of molecular sciences · 2025
    Review
  4. Review
  5. Article
  6. Greatwall-Endos-PP2A/B55Open biology · 2024
    Article
  7. Article
  8. Article
  9. Review
  10. The ATM-E6AP-MASTL axis mediates DNA damage checkpoint recovery.bioRxiv : the preprint server for biology · 2023
    Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Review
  16. Dephosphorylation in nuclear reassembly after mitosis.Frontiers in cell and developmental biology · 2022
    Review
  17. Article
  18. Article
  19. Article
  20. Article

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

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

5 authors at 2 institutions in 2 countries.

Priscila V CastilhoDepartment of Molecular Biology and Genetics, Cornell University, Ithaca, NY 14853, USA.
Byron C Williams
Satoru Mochida
Yong Zhao
Michael L Goldberg
Cornell University · USCancer Research UK · GB

Funding

Greatwall Kinase and the Mitotic Control of Phosphatase ActivityR01GM048430 · NIGMS · CORNELL UNIVERSITY ITHACA · PI GOLDBERG, MICHAEL L · 1992 to 2017
$6.6M
NIGMS NIH HHS GM48430NIGMS NIH HHS R01 GM048430
6 · The paper itself

Abstract

We have previously shown that Greatwall kinase (Gwl) is required for M phase entry and maintenance in Xenopus egg extracts. Here, we demonstrate that Gwl plays a crucial role in a novel biochemical pathway that inactivates, specifically during M phase, "antimitotic" phosphatases directed against phosphorylations catalyzed by cyclin-dependent kinases (CDKs). A major component of this phosphatase activity is heterotrimeric PP2A containing the B55delta regulatory subunit. Gwl is activated during M phase by Cdk1/cyclin B (MPF), but once activated, Gwl promotes PP2A/B55delta inhibition with no further requirement for MPF. In the absence of Gwl, PP2A/B55delta remains active even when MPF levels are high. The removal of PP2A/B55delta corrects the inability of Gwl-depleted extracts to enter M phase. These findings support the hypothesis that M phase requires not only high levels of MPF function, but also the suppression, through a Gwl-dependent mechanism, of phosphatase(s) that would otherwise remove MPF-driven phosphorylations.

Indexed as

AnimalsCalcineurinCalcium-Calmodulin-Dependent Protein Kinase Type 2Cell DivisionCyclin-Dependent KinasesEnzyme InhibitorsMaturation-Promoting FactorOkadaic AcidOocytesPhosphorylationProtein Phosphatase 2Protein Serine-Threonine KinasesProtein SubunitsXenopus laevisXenopus ProteinsCalcineurinCalcium-Calmodulin-Dependent Protein Kinase Type 2Cyclin-Dependent KinasesEnzyme InhibitorsMASTL protein, XenopusMaturation-Promoting FactorOkadaic AcidProtein Phosphatase 2Protein Serine-Threonine KinasesProtein SubunitsXenopus Proteins

Identifiers

PMID19793917
PMCPMC2777107
OpenAlexW2149870815

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.