Evidence map›Paper›PMID 18801733›Full record

ArticleThe Journal of biological chemistry2008

A Trypanosoma cruzi phosphatidylinositol 3-kinase (TcVps34) is involved in osmoregulation and receptor-mediated endocytosis.

Alejandra C Schoijet, Kildare Miranda, Wendell Girard-Dias, Wanderley de Souza, Mirtha M Flawiá, Héctor N Torres, Roberto Docampo, Guillermo D Alonso

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed, 1 pooled it
2.4field-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

24 citing papers in PubMed, 1 synthesis or guideline pooled it, 49 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

8 authors at 4 institutions in 3 countries.

Alejandra C SchoijetInstituto de Investigaciones en Ingeniería Genética y Biología Molecular, Consejo Nacional de Investigaciones Científicas yTécnicas, Universidad de Buenos Aires, Vuelta de Obligado 2490 (1428), Buenos Aires, Argentina.
Kildare Miranda
Wendell Girard-Dias
Wanderley de Souza
Mirtha M Flawiá
Héctor N Torres
Roberto Docampo
Guillermo D Alonso
Universidade Federal do Rio de Janeiro · BRConsejo Nacional de Investigaciones Científicas y Técnicas · ARUniversity of Georgia · USUniversity of Buenos Aires · AR

Funding

The contractile vacuole of Trypanosoma cruziR01AI068647 · NIAID · UNIVERSITY OF GEORGIA · PI DOCAMPO, ROBERTO · 2006 to 2010
$1.8M
NIAID NIH HHS AI-68647NIAID NIH HHS R01 AI068647
6 · The paper itself

Abstract

Trypanosoma cruzi, the etiological agent of Chagas disease, has the ability to respond to a variety of environmental changes during its life cycle both in the insect vector and in the vertebrate host. Because regulation of transcription initiation seems to be nonfunctional in this parasite, it is important to investigate other regulatory mechanisms of adaptation. Regulatory mechanisms at the level of signal transduction pathways involving phosphoinositides are good candidates for this purpose. Here we report the identification of the first phosphatidylinositol 3-kinase (PI3K) in T. cruzi, with similarity with its yeast counterpart, Vps34p. TcVps34 specifically phosphorylates phosphatidylinositol to produce phosphatidylinositol 3-phosphate, thus confirming that it belongs to class III PI3K family. Overexpression of TcVps34 resulted in morphological and functional alterations related to vesicular trafficking. Although inhibition of TcVps34 with specific PI3K inhibitors, such as wortmannin and LY294,000, resulted in reduced regulatory volume decrease after hyposmotic stress, cells overexpressing this enzyme were resistant to these inhibitors. Furthermore, these cells were able to recover their original volume faster than wild type cells when they were submitted to severe hyposmotic stress. In addition, in TcVps34-overexpressing cells, the activities of vacuolar-H+-ATPase and vacuolar H+-pyrophosphatase were altered, suggesting defects in the acidification of intracellular compartments. Furthermore, receptor-mediated endocytosis was partially blocked although fluid phase endocytosis was not affected, confirming a function for TcVps34 in membrane trafficking. Taken together, these results strongly support that TcVps34 plays a prominent role in vital processes for T. cruzi survival such as osmoregulation, acidification, and vesicular trafficking.

Indexed as

EndocytosisWater-Electrolyte BalanceAnimalsCloning, MolecularGene Expression Regulation, EnzymologicInorganic PyrophosphataseMicroscopy, Electron, ScanningMicroscopy, Electron, TransmissionMolecular Sequence DataPhenotypePhosphatidylinositol 3-KinasesPhosphoinositide-3 Kinase InhibitorsProtein Kinase InhibitorsProton-Translocating ATPasesSaccharomyces cerevisiaeTrypanosoma cruziInorganic PyrophosphatasePhosphatidylinositol 3-KinasesPhosphoinositide-3 Kinase InhibitorsProtein Kinase InhibitorsProton-Translocating ATPases

Identifiers

PMID18801733
PMCPMC2581564
OpenAlexW2033538590

What OpenQuestion holds

Textmetadata
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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.