Evidence map›Paper›PMID 11904383›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2002

Actions of PP2A on the MAP kinase pathway and apoptosis are mediated by distinct regulatory subunits.

Adam M Silverstein, Christina A Barrow, Anthony J Davis, Marc C Mumby

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 128 papers.

0numbers the graph read from it
0cells of the map it votes in
128citing papers in PubMed
6.7field-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

128 citing papers in PubMed, 272 citations in OpenAlex.

  1. Article
  2. Nitration in cancer signaling.Redox biology · 2026
    Review
  3. Article
  4. Targeting PP2A in cancer: an underrated option.Journal of experimental & clinical cancer research : CR · 2025
    Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Regulation of Cardiac PKA Signaling by cAMP and Oxidants.Antioxidants (Basel, Switzerland) · 2021
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review

68 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

4 authors at 2 institutions in 1 country.

Adam M SilversteinDepartment of Pharmacology, University of Texas Southwestern Medical Center, Dallas, TX 75390-9041, USA.
Christina A Barrow
Anthony J Davis
Marc C Mumby
The University of Texas Southwestern Medical Center · USRadiation Oncology Associates · US

Funding

REGULATION OF PROTEIN DEPHOSPHROYLATIONR01GM049505 · NIGMS · UNIVERSITY OF TEXAS SW MED CTR/DALLAS · PI MUMBY, MARC C. · 1994 to 2005
$1.8M
FUNCTIONAL ROLES OF THE PP2A REGULATORY SUBUNITSF32GM020530 · NIGMS · UNIVERSITY OF TEXAS SW MED CTR/DALLAS · PI SILVERSTEIN, ADAM M · 2000 to 2001
$73k
NIGMS NIH HHS F32 GM020530NIGMS NIH HHS GM20530NIGMS NIH HHS GM49505NIGMS NIH HHS R01 GM049505
6 · The paper itself

Abstract

Individual subunits of protein phosphatase 2A (PP2A), protein phosphatase 4, and protein phosphatase 5 were knocked out in Drosophila Schneider 2 cells by using RNA interference. Ablation of either the scaffold (A) or catalytic (C) subunits of PP2A caused the disappearance of all PP2A subunits. Treating cells with double-stranded RNA targeting all four of the Drosophila PP2A regulatory subunits caused the disappearance of both the A and C subunits. The loss of PP2A subunits was associated with decreased protein stability indicating that only the heterotrimeric forms of PP2A are stable in intact cells. Ablation of total PP2A by using double-stranded RNA against either the A or C subunit, or specific ablation of the R2/B regulatory subunit, enhanced insulin-induced ERK activation. These results indicated that the R2/B subunit targets PP2A to the mitogen-activated protein (MAP) kinase cascade in Schneider 2 cells, where it acts as a negative regulator. A severe loss of viability occurred in cells in which total PP2A or both isoforms of the Drosophila R5/B56 subunit had been ablated. The reduced viability of these cells correlated with the induction of markers of apoptosis including membrane blebbing and stimulation of caspase-3-like activity. These observations indicated that PP2A has a powerful antiapoptotic activity that is specifically mediated by the R5/B56 regulatory subunits. In contrast to PP2A, ablation of protein phosphatase 4 caused only a slight reduction in cell growth but had no effect on MAP kinase signaling or apoptosis. Depletion of protein phosphatase 5 had no effects on MAP kinase, cell growth, or apoptosis.

Indexed as

ApoptosisAnimalsCells, CulturedDrosophilaEnzyme ActivationMAP Kinase Signaling SystemPhosphoprotein PhosphatasesProtein Phosphatase 2Protein SubunitsRNA, Double-StrandedPhosphoprotein PhosphatasesProtein Phosphatase 2Protein SubunitsRNA, Double-Stranded

Identifiers

PMID11904383
PMCPMC123629
OpenAlexW2101803513

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.