Evidence map›Paper›PMID 30976120›Full record

ArticleScientific reports2019

A plasma membrane localized protein phosphatase in Toxoplasma gondii, PPM5C, regulates attachment to host cells.

Chunlin Yang, Malgorzata Broncel, Caia Dominicus, Emily Sampson, William J Blakely, Moritz Treeck, Gustavo Arrizabalaga

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
3.2field-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

25 citing papers in PubMed, 45 citations in OpenAlex.

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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

7 authors at 2 institutions in 2 countries.

Chunlin YangDepartment of Pharmacology and Toxicology, Indiana University School of Medicine, Indianapolis, IN, USA.
Malgorzata BroncelSignalling in Apicomplexan Parasites Laboratory, The Francis Crick Institute, London, United Kingdom.
Caia DominicusSignalling in Apicomplexan Parasites Laboratory, The Francis Crick Institute, London, United Kingdom.
Emily SampsonDepartment of Pharmacology and Toxicology, Indiana University School of Medicine, Indianapolis, IN, USA.
William J BlakelyDepartment of Pharmacology and Toxicology, Indiana University School of Medicine, Indianapolis, IN, USA.
Moritz TreeckSignalling in Apicomplexan Parasites Laboratory, The Francis Crick Institute, London, United Kingdom.ORCID http://orcid.org/0000-0002-7883-6743
Gustavo ArrizabalagaDepartment of Pharmacology and Toxicology, Indiana University School of Medicine, Indianapolis, IN, USA. garrizab@iu.edu.
Indiana University School of MedicineThe Francis Crick Institute · GB

Funding

Dissecting a novel mechanism of drug-induced death in Toxoplasma gondiiR01AI089808 · NIAID · UNIVERSITY OF IDAHO · PI ARRIZABALAGA, GUSTAVO A · 2010 to 2013
$882k
NIAID NIH HHS R01 AI089808
6 · The paper itself

Abstract

The propagation of Toxoplasma gondii is accomplished by repeated lytic cycles of parasite attachment to a host cell, invasion, replication within a parasitophorous vacuole, and egress from the cell. This lytic cycle is delicately regulated by calcium-dependent reversible phosphorylation of the molecular machinery that drives invasion and egress. While much progress has been made elucidating the protein kinases and substrates central to parasite propagation, little is known about the relevant protein phosphatases. In this study, we focused on the five protein phosphatases that are predicted to be membrane-associated either integrally or peripherally. We have determined that of these only PPM5C, a PP2C family member, localizes to the plasma membrane of Toxoplasma. Disruption of PPM5C results in a slow propagation phenotype in tissue culture. Interestingly, parasites lacking PPM5C divide and undergo egress at a normal rate, but have a deficiency in attaching to host cells. Both membrane localization and phosphatase activity are required for PPM5C's role in attachment. Phosphoproteomic analysis show relatively few phosphorylation sites being affected by PPM5C deletion in extracellular parasites of which several are found on proteins involved in signaling cascades. This implies that PPM5C is part of a wider regulatory network important for attachment to host cells.

Indexed as

Host-Parasite InteractionsCalcium SignalingCell-Matrix JunctionsCell MembraneFibroblastsHumansPhosphoprotein PhosphatasesPhosphorylationProtozoan ProteinsToxoplasmaToxoplasmosisPhosphoprotein PhosphatasesProtozoan Proteins

Identifiers

PMID30976120
PMCPMC6459975
OpenAlexW2939882826

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.