Evidence map›Paper›PMID 31349904›Full record

ReviewAdvances in cancer research2019

PP2A holoenzymes, substrate specificity driving cellular functions and deregulation in cancer.

Holly Fowle, Ziran Zhao, Xavier Graña

Open access · greenAbstract readReview
In one paragraph

Review in Advances in cancer research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
11.3field-weighted citation impact, top 1% 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

51 citing papers in PubMed, 91 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Targeting PP2A in cancer: an underrated option.Journal of experimental & clinical cancer research : CR · 2025
    Review
  10. Article
  11. Article
  12. Article
  13. Protein phosphatases in systemic autoimmunity.Immunometabolism (Cobham, Surrey) · 2025
    Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  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

3 authors at 1 institution in 1 country.

Holly FowleFels Institute for Cancer Research and Molecular Biology and Temple University Lewis Katz School of Medicine, Philadelphia, PA, United States.
Ziran ZhaoFels Institute for Cancer Research and Molecular Biology and Temple University Lewis Katz School of Medicine, Philadelphia, PA, United States.
Xavier GrañaFels Institute for Cancer Research and Molecular Biology and Temple University Lewis Katz School of Medicine, Philadelphia, PA, United States. Electronic address: xgrana@temple.edu.
Temple University · US

Funding

WORD PROCESSING CENTER--COREP30CA006927 · NCI · RESEARCH INST OF FOX CHASE CAN CTR · PI Margaret von Mehren · 1985 to 2026
$138.8M
Unraveling the complexity of substrate specificity of PP2A/B55a, a major eukaryote Serine/Threonine PhosphataseR01GM117437 · NIGMS · TEMPLE UNIV OF THE COMMONWEALTH · PI GRANA, XAVIER · 2016 to 2019
$1.3M
PPP2R2A tumor suppression haploinsufficiency in prostate cancerR03CA216134 · NCI · TEMPLE UNIV OF THE COMMONWEALTH · PI GRANA, XAVIER · 2017 to 2018
$159k
NCI NIH HHS P30 CA006927NCI NIH HHS R03 CA216134NIGMS NIH HHS R01 GM117437
6 · The paper itself

Abstract

PP2A is a highly conserved eukaryotic serine/threonine protein phosphatase of the PPP family of phosphatases with fundamental cellular functions. In cells, PP2A targets specific subcellular locations and substrates by forming heterotrimeric holoenzymes, where a core dimer consisting of scaffold (A) and catalytic (C) subunits complexes with one of many B regulatory subunits. PP2A plays a key role in positively and negatively regulating a myriad of cellular processes, as it targets a very sizable fraction of the cellular substrates phosphorylated on Ser/Thr residues. This review focuses on insights made toward the understanding on how the subunit composition and structure of PP2A holoenzymes mediates substrate specificity, the role of substrate modulation in the signaling of cellular division, growth, and differentiation, and its deregulation in cancer.

Indexed as

AnimalsCell CycleCell DifferentiationCell ProliferationHoloenzymesHumansNeoplasmsPhosphorylationProtein Phosphatase 2Signal TransductionSubstrate SpecificityHoloenzymesProtein Phosphatase 2B55αCancerCell cyclep107PhosphorylationPP2A holoenzymePPP2R2ARetinoblastoma protein (pRB)Serine/threonine protein phosphatasesSubstrate specificity

Identifiers

PMID31349904
PMCPMC9994639
OpenAlexW2939469066

What OpenQuestion holds

Textmetadata
LicenceTDM
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.