Evidence map›Paper›PMID 34686773›Full record

ReviewOncogene2022

PP2A-B55: substrates and regulators in the control of cellular functions.

Priya Amin, Sushil Awal, Suzanne Vigneron, Sylvain Roque, Francisca Mechali, Jean Claude Labbé, Thierry Lorca, Anna Castro

Abstract readReview
PubMed Publisher
In one paragraph

Review in Oncogene, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.6field-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

23 citing papers in PubMed, 43 citations in OpenAlex.

  1. Article
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  3. Houge-Janssens syndrome.European journal of human genetics : EJHG · 2025
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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

8 authors at 1 institution in 1 country.

Priya AminCentre de Recherche en Biologie Cellulaire de Montpellier (CRBM), CNRS UMR 5237, Université de Montpellier, 1919 Route de Mende, Montpellier Cedex 5, Montpellier, 34293, France.
Sushil AwalCentre de Recherche en Biologie Cellulaire de Montpellier (CRBM), CNRS UMR 5237, Université de Montpellier, 1919 Route de Mende, Montpellier Cedex 5, Montpellier, 34293, France.
Suzanne VigneronCentre de Recherche en Biologie Cellulaire de Montpellier (CRBM), CNRS UMR 5237, Université de Montpellier, 1919 Route de Mende, Montpellier Cedex 5, Montpellier, 34293, France.
Sylvain RoqueCentre de Recherche en Biologie Cellulaire de Montpellier (CRBM), CNRS UMR 5237, Université de Montpellier, 1919 Route de Mende, Montpellier Cedex 5, Montpellier, 34293, France.
Francisca MechaliCentre de Recherche en Biologie Cellulaire de Montpellier (CRBM), CNRS UMR 5237, Université de Montpellier, 1919 Route de Mende, Montpellier Cedex 5, Montpellier, 34293, France.
Jean Claude LabbéCentre de Recherche en Biologie Cellulaire de Montpellier (CRBM), CNRS UMR 5237, Université de Montpellier, 1919 Route de Mende, Montpellier Cedex 5, Montpellier, 34293, France.
Thierry LorcaCentre de Recherche en Biologie Cellulaire de Montpellier (CRBM), CNRS UMR 5237, Université de Montpellier, 1919 Route de Mende, Montpellier Cedex 5, Montpellier, 34293, France. thierry.lorca@crbm.cnrs.fr.ORCID http://orcid.org/0000-0003-2007-8924
Anna CastroCentre de Recherche en Biologie Cellulaire de Montpellier (CRBM), CNRS UMR 5237, Université de Montpellier, 1919 Route de Mende, Montpellier Cedex 5, Montpellier, 34293, France. anna.castro@crbm.cnrs.fr.ORCID http://orcid.org/0000-0002-3655-1352
Centre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

PP2A is a major serine/threonine phosphatase class involved in the regulation of cell signaling through the removal of protein phosphorylation. This class of phosphatases is comprised of different heterotrimeric complexes displaying distinct substrate specificities. The present review will focus on one specific heterocomplex, the phosphatase PP2A-B55. Herein, we will report the direct substrates of this phosphatase identified to date, and its impact on different cell signaling cascades. We will additionally describe its negative regulation by its inhibitors Arpp19 and ENSA and their upstream kinase Greatwall. Finally, we will describe the essential molecular features defining PP2A-B55 substrate specificity that confer the correct temporal pattern of substrate dephosphorylation. The main objective of this review is to provide the reader with a unique source compiling all the knowledge of this particular holoenzyme that has evolved as a key enzyme for cell homeostasis and cancer development.

Indexed as

HumansProtein Phosphatase 2Signal TransductionProtein Phosphatase 2

Identifiers

PMID34686773
OpenAlexW3207898098

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.