Evidence map›Paper›PMID 25536081›Full record

ArticlePloS one2014

Visualization of subunit interactions and ternary complexes of protein phosphatase 2A in mammalian cells.

Shu-Ting Mo, Shang-Ju Chiang, Tai-Yu Lai, Yu-Ling Cheng, Cheng-En Chung, Spencer C H Kuo, Kelie M Reece, Yung-Cheng Chen, Nan-Shan Chang, Brian E Wadzinski and 1 more

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
2.1field-weighted citation impact, top 12% 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

10 citing papers in PubMed, 15 citations in OpenAlex.

  1. Article
  2. Targeting PP2A in cancer: an underrated option.Journal of experimental & clinical cancer research : CR · 2025
    Review
  3. JNK Cascade-Induced Apoptosis-A Unique Role in GqPCR Signaling.International journal of molecular sciences · 2023
    Review
  4. Article
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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

11 authors at 2 institutions in 2 countries.

Shu-Ting MoInstitute of Molecular Medicine, College of Medicine, National Cheng Kung University, Tainan, Taiwan.
Shang-Ju ChiangInstitute of Molecular Medicine, College of Medicine, National Cheng Kung University, Tainan, Taiwan.
Tai-Yu LaiInstitute of Basic Medical Sciences, College of Medicine, National Cheng Kung University, Tainan, Taiwan.
Yu-Ling ChengInstitute of Molecular Medicine, College of Medicine, National Cheng Kung University, Tainan, Taiwan.
Cheng-En ChungInstitute of Molecular Medicine, College of Medicine, National Cheng Kung University, Tainan, Taiwan.
Spencer C H KuoDepartment of Medicine, College of Medicine, National Cheng Kung University, Tainan, Taiwan.
Kelie M ReeceDepartment of Pharmacology, Vanderbilt University Medical Center, Nashville, TN, United States of America.
Yung-Cheng ChenInstitute of Molecular Medicine, College of Medicine, National Cheng Kung University, Tainan, Taiwan.
Nan-Shan ChangInstitute of Molecular Medicine, College of Medicine, National Cheng Kung University, Tainan, Taiwan; Institute of Basic Medical Sciences, College of Medicine, National Cheng Kung University, Tainan, Taiwan; Center for Infectious Disease and Signaling Research, National Cheng Kung University, Tainan, Taiwan.
Brian E WadzinskiDepartment of Pharmacology, Vanderbilt University Medical Center, Nashville, TN, United States of America.
Chi-Wu ChiangInstitute of Molecular Medicine, College of Medicine, National Cheng Kung University, Tainan, Taiwan; Institute of Basic Medical Sciences, College of Medicine, National Cheng Kung University, Tainan, Taiwan; Center for Infectious Disease and Signaling Research, National Cheng Kung University, Tainan, Taiwan.
National Cheng Kung University · TWVanderbilt University Medical Center · US

Funding

Structure and function of protein kinase/PP2A complexesR01GM051366 · NIGMS · VANDERBILT UNIVERSITY · PI WADZINSKI, BRIAN E · 1994 to 2011
$2.9M
Structure and function of protein kinase/PP2A complexesR56GM051366 · NIGMS · VANDERBILT UNIVERSITY · PI WADZINSKI, BRIAN E · 2007 to 2007
$349k
NIGMS NIH HHS GM051366NIGMS NIH HHS R01 GM051366NIGMS NIH HHS R56 GM051366
6 · The paper itself

Abstract

Protein phosphatase 2A (PP2A) is a ubiquitous phospho-serine/threonine phosphatase that controls many diverse cellular functions. The predominant form of PP2A is a heterotrimeric holoenzyme consisting of a scaffolding A subunit, a variable regulatory B subunit, and a catalytic C subunit. The C subunit also associates with other interacting partners, such as α4, to form non-canonical PP2A complexes. We report visualization of PP2A complexes in mammalian cells. Bimolecular fluorescence complementation (BiFC) analysis of PP2A subunit interactions demonstrates that the B subunit plays a key role in directing the subcellular localization of PP2A, and confirms that the A subunit functions as a scaffold in recruiting the B and C subunits to form a heterotrimeric holoenzyme. BiFC analysis also reveals that α4 promotes formation of the AC core dimer. Furthermore, we demonstrate visualization of specific ABC holoenzymes in cells by combining BiFC and fluorescence resonance energy transfer (BiFC-FRET). Our studies not only provide direct imaging data to support previous biochemical observations on PP2A complexes, but also offer a promising approach for studying the spatiotemporal distribution of individual PP2A complexes in cells.

Indexed as

AnimalsFluorescent Antibody TechniqueMiceNIH 3T3 CellsProtein MultimerizationProtein Phosphatase 2Protein SubunitsProtein Phosphatase 2Protein Subunits

Identifiers

PMID25536081
PMCPMC4275284
OpenAlexW2000593949

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.