Evidence map›Paper›PMID 21852956›Full record

ArticlePLoS genetics2011

Suppression of scant identifies Endos as a substrate of greatwall kinase and a negative regulator of protein phosphatase 2A in mitosis.

Hélène Rangone, Eva Wegel, Melanie K Gatt, Eirene Yeung, Alexander Flowers, Janusz Debski, Michal Dadlez, Veerle Janssens, Adelaide T C Carpenter, David M Glover

Open access · goldAbstract read
In one paragraph

Article in PLoS genetics, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
3.8field-weighted citation impact, top 7% 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

43 citing papers in PubMed, 61 citations in OpenAlex.

  1. Article
  2. Greatwall-Endos-PP2A/B55Open biology · 2024
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

10 authors at 3 institutions in 3 countries.

Hélène RangoneDepartment of Genetics, University of Cambridge, Cambridge, United Kingdom.
Eva Wegel
Melanie K Gatt
Eirene Yeung
Alexander Flowers
Janusz Debski
Michal Dadlez
Veerle Janssens
Adelaide T C Carpenter
David M Glover
University of Cambridge · GBInstitute of Biochemistry and Biophysics, Polish Academy of Sciences · PLKU Leuven · BE

Funding

Minority Health and Health Disparities International Research Training ProgramT37MD001368 · NIMHD · CALIFORNIA STATE UNIVERSITY FULLERTON · PI TOLMASKY, MARCELO E · 2005 to 2024
$3.9M
Medical Research Council G0501718Medical Research Council G1001696NIMHD NIH HHS T37 MD001368
6 · The paper itself

Abstract

Protein phosphatase 2A (PP2A) plays a major role in dephosphorylating the targets of the major mitotic kinase Cdk1 at mitotic exit, yet how it is regulated in mitotic progression is poorly understood. Here we show that mutations in either the catalytic or regulatory twins/B55 subunit of PP2A act as enhancers of gwl(Scant), a gain-of-function allele of the Greatwall kinase gene that leads to embryonic lethality in Drosophila when the maternal dosage of the mitotic kinase Polo is reduced. We also show that heterozygous mutant endos alleles suppress heterozygous gwl(Scant); many more embryos survive. Furthermore, heterozygous PP2A mutations make females heterozygous for the strong mutation polo(11) partially sterile, even in the absence of gwl(Scant). Heterozygosity for an endos mutation suppresses this PP2A/polo(11) sterility. Homozygous mutation or knockdown of endos leads to phenotypes suggestive of defects in maintaining the mitotic state. In accord with the genetic interactions shown by the gwl(Scant) dominant mutant, the mitotic defects of Endos knockdown in cultured cells can be suppressed by knockdown of either the catalytic or the Twins/B55 regulatory subunits of PP2A but not by the other three regulatory B subunits of Drosophila PP2A. Greatwall phosphorylates Endos at a single site, Ser68, and this is essential for Endos function. Together these interactions suggest that Greatwall and Endos act to promote the inactivation of PP2A-Twins/B55 in Drosophila. We discuss the involvement of Polo kinase in such a regulatory loop.

Indexed as

MitosisMutationAnimalsCells, CulturedDrosophila melanogasterDrosophila ProteinsFemaleFertilityGene Knockdown TechniquesGene Regulatory NetworksGenetic Association StudiesLarvaMaleMicroscopy, FluorescenceNervous SystemPeptidesDrosophila Proteinsendos protein, DrosophilaGwl protein, DrosophilaPeptidesPhosphoprotein Phosphatasespolo protein, DrosophilaProtein Serine-Threonine Kinasestws protein, Drosophila

Identifiers

PMID21852956
PMCPMC3154957
OpenAlexW2041200270

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.