Evidence map›Paper›PMID 40901993›Full record

ArticlePLoS pathogens2025

The PP2A-2 holoenzyme orchestrates daughter cell emergence during cytokinesis in Toxoplasma gondii.

Jin-Lei Wang, Meng Wang, Nian-Zhang Zhang, Ting-Ting Li, Jin Gao, Xiao-Jing Wu, Bao-Quan Fu, Hany M Elsheikha, Xing-Quan Zhu

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in PLoS pathogens, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

9 authors.

Jin-Lei WangState Key Laboratory for Animal Disease Control and Prevention, College of Veterinary Medicine, Lanzhou University, Lanzhou Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Lanzhou, China.
Meng WangState Key Laboratory for Animal Disease Control and Prevention, College of Veterinary Medicine, Lanzhou University, Lanzhou Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Lanzhou, China.
Nian-Zhang ZhangState Key Laboratory for Animal Disease Control and Prevention, College of Veterinary Medicine, Lanzhou University, Lanzhou Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Lanzhou, China.
Ting-Ting LiState Key Laboratory for Animal Disease Control and Prevention, College of Veterinary Medicine, Lanzhou University, Lanzhou Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Lanzhou, China.
Jin GaoState Key Laboratory for Animal Disease Control and Prevention, College of Veterinary Medicine, Lanzhou University, Lanzhou Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Lanzhou, China.
Xiao-Jing WuState Key Laboratory for Animal Disease Control and Prevention, College of Veterinary Medicine, Lanzhou University, Lanzhou Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Lanzhou, China.
Bao-Quan FuState Key Laboratory for Animal Disease Control and Prevention, College of Veterinary Medicine, Lanzhou University, Lanzhou Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Lanzhou, China.
Hany M ElsheikhaFaculty of Medicine and Health Sciences, School of Veterinary Medicine and Science, University of Nottingham, Loughborough, United Kingdom.
Xing-Quan ZhuLaboratory of Parasitic Diseases, College of Veterinary Medicine, Shanxi Agricultural University, Taigu, China.ORCID 0000-0003-2530-4628

Funding

National Key Research and Development Program of ChinaNational Natural Science Foundation of ChinaNatural Science Foundation of Gansu Province, China
6 · The paper itself

Abstract

Toxoplasma gondii is a significant pathogen in both humans and animals, with disease progression driven by the rapid proliferation of its tachyzoite stage. In this study, we identify the PP2A-2 holoenzyme as a key regulator of daughter cell emergence during parasite division. This holoenzyme, likely composed of the regulatory subunit TgPR48 (PP2A-B2), the catalytic subunit PP2A-C2, and the scaffolding subunit PP2A-A2, is essential for proper cytokinesis. Disruption of any single component severely impairs daughter cell separation and emergence. Phosphoproteomic analysis following PP2A-C2 depletion revealed numerous differentially phosphorylated proteins. Among these, DCS1 and DCS2 were prioritized as potential effectors. While phosphomimetic and non-phosphorylatable mutations in DCS1 and DCS2 did not significantly impair their function, depletion of either protein disrupted TgPR48 localization. Interestingly, TgPR48 overexpression partially rescued the phenotypes associated with DCS2 loss, but not DCS1, indicating divergence in their downstream pathways and implicating additional, yet unidentified, substrates. These findings establish PP2A-2-mediated dephosphorylation as a central mechanism in regulating tachyzoite cytokinesis and highlight a promising regulatory axis for therapeutic intervention against T. gondii.

Indexed as

CytokinesisProtein Phosphatase 2Protozoan ProteinsToxoplasmaToxoplasmosisAnimalsHumansPhosphorylationProtein Phosphatase 2Protozoan Proteins

Identifiers

PMID40901993
PMCPMC12425318

What Socratic 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 Socratic graph.