Evidence map›Paper›PMID 22469975›Full record

ReviewOncogene2013

The Greatwall kinase: a new pathway in the control of the cell cycle.

T Lorca, A Castro

Open access · bronzeAbstract readReview
PubMed Publisher
In one paragraph

Review in Oncogene, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
3.1field-weighted citation impact, top 9% 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, 63 citations in OpenAlex.

  1. Review
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  16. Review
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  18. The Oncogenic Functions of MASTL Kinase.Frontiers in cell and developmental biology · 2018
    Review
  19. Review
  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

2 authors at 1 institution in 1 country.

T LorcaCentre de Recherche de Biochimie Macromoléculaire, CNRS UMR 5237, Universités Montpellier 2 et 1, Montpellier, France. thierry.lorca@crbm.cnrs.fr
A Castro
Centre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

New data have recently established that protein phosphorylation during mitosis is the result of a controlled balance between kinase and phosphatase activities and that, as for mitotic kinases, phosphatases are also regulated during cell division. This regulation is at least in part induced by the activation of the Greatwall (Gwl) kinase at mitotic entry. Activated Gwl phosphorylates its substrates cAMP-regulated phospho protein 19 (Arpp19) and α-endosulfine (ENSA), promoting their binding to and the inhibition of PP2A. Interestingly, besides the role of the Gwl-Arpp19/ENSA in the control of mitotic division, new data in yeast support the involvement of this pathway in mRNA stabilization during G(0) program initiation, although in this case the phosphatase PP2A appears not to be implicated. Finally, Gwl activity has been shown to be required for DNA checkpoint recovery. These new findings support the view that Gwl, Arpp19 and ENSA could function as the core of a new signalization pathway that, by targeting different final substrates, could participate in a variety of physiological functions.

Indexed as

AnimalsCell CycleDrosophila ProteinsGenomic InstabilityIntercellular Signaling Peptides and ProteinsMitosisPeptidesPhosphoproteinsPhosphorylationProtein Serine-Threonine KinasesRNA, MessengerSignal Transductioncyclic AMP-regulated phosphoprotein 19Drosophila ProteinsendosulfineGwl protein, DrosophilaIntercellular Signaling Peptides and ProteinsPeptidesPhosphoproteinsProtein Serine-Threonine KinasesRNA, Messenger

Identifiers

PMID22469975
OpenAlexW1982832729

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.