Evidence map›Paper›PMID 28298606›Full record

ArticleJournal of virology2017

Dengue Virus Activates the AMP Kinase-mTOR Axis To Stimulate a Proviral Lipophagy.

Tristan X Jordan, Glenn Randall

Open access · bronzeAbstract read
In one paragraph

Article in Journal of virology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 80 papers.

0numbers the graph read from it
0cells of the map it votes in
80citing papers in PubMed
9.1field-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

80 citing papers in PubMed, 125 citations in OpenAlex.

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  20. Multiple receptor tyrosine kinases regulate dengue infection of hepatocytes.Frontiers in cellular and infection microbiology · 2024
    Article

20 more citing papers are in PubMed but not listed here.

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

2 authors at 1 institution in 1 country.

Tristan X JordanDepartment of Microbiology, The University of Chicago, Chicago, Illinois, USA.
Glenn RandallDepartment of Microbiology, The University of Chicago, Chicago, Illinois, USA grandall@bsd.uchicago.edu.
University of Chicago · US

Funding

Molecular And Cellular Biology Training ProgramT32GM007183 · NIGMS · UNIVERSITY OF CHICAGO · PI GLICK, BENJAMIN S, RICE, PHOEBE A · 1985 to 2021
$23.9M
Hepatitis C Virus Trafficking in Infected HepatocytesR01AI080703 · NIAID · UNIVERSITY OF CHICAGO · PI RANDALL, GLENN C · 2010 to 2014
$1.7M
HEPATOCYTE REMODELING BY HEPATITIS C VIRUSR01DK102883 · NIDDK · UNIVERSITY OF CHICAGO · PI RANDALL, GLENN C · 2015 to 2018
$1.4M
NIAID NIH HHS R01 AI080703NIDDK NIH HHS R01 DK102883NIGMS NIH HHS T32 GM007183
6 · The paper itself

Abstract

Robust dengue virus (DENV) replication requires lipophagy, a selective autophagy that targets lipid droplets. The autophagic mobilization of lipids leads to increased β-oxidation in DENV-infected cells. The mechanism by which DENV induces lipophagy is unknown. Here, we show that infection with DENV activates the metabolic regulator 5' adenosine-monophosphate activated kinase (AMPK), and that the silencing or pharmacological inhibition of AMPK activity decreases DENV replication and the induction of lipophagy. The activity of the mechanistic target of rapamycin complex 1 (mTORC1) decreases in DENV-infected cells and is inversely correlated with lipophagy induction. Constitutive activation of mTORC1 by depletion of tuberous sclerosis complex 2 (TSC2) inhibits lipophagy induction in DENV-infected cells and decreases viral replication. While AMPK normally stimulates TSC2-dependent inactivation of mTORC1 signaling, mTORC1 inactivation is independent of AMPK activation during DENV infection. Thus, DENV stimulates and requires AMPK signaling as well as AMPK-independent suppression of mTORC1 activity for proviral lipophagy.

Indexed as

AutophagyLipid MetabolismAdenylate KinaseDengue VirusDNA ReplicationGene Expression Regulation, ViralHEK293 CellsHep G2 CellsHumansMechanistic Target of Rapamycin Complex 1Multiprotein ComplexesProvirusesSignal TransductionTOR Serine-Threonine KinasesTuberous Sclerosis Complex 2 ProteinTumor Suppressor ProteinsAdenylate KinaseMechanistic Target of Rapamycin Complex 1Multiprotein ComplexesTOR Serine-Threonine KinasesTSC2 protein, humanTuberous Sclerosis Complex 2 ProteinTumor Suppressor Proteinsautophagylipid metabolism

Identifiers

PMID28298606
PMCPMC5432877
OpenAlexW2613882318

What OpenQuestion holds

Textmetadata
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.