Evidence map›Paper›PMID 30715798›Full record

ArticleThe FEBS journal2019

MAVS polymers smaller than 80 nm induce mitochondrial membrane remodeling and interferon signaling.

Ming-Shih Hwang, Jérôme Boulanger, Jonathan D Howe, Anna Albecka, Mathias Pasche, Leila Mureşan, Yorgo Modis

Open access · hybridAbstract read
In one paragraph

Article in The FEBS journal, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.1field-weighted citation impact, top 23% 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

18 citing papers in PubMed, 26 citations in OpenAlex.

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  6. Multifaceted mitochondria in innate immunity.npj metabolic health and disease · 2024
    Review
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 2 institutions in 1 country.

Ming-Shih HwangDepartment of Medicine, University of Cambridge, MRC Laboratory of Molecular Biology, UK.
Jérôme BoulangerMRC Laboratory of Molecular Biology, Cambridge, UK.
Jonathan D HoweMRC Laboratory of Molecular Biology, Cambridge, UK.
Anna AlbeckaDepartment of Medicine, University of Cambridge, MRC Laboratory of Molecular Biology, UK.
Mathias PascheMRC Laboratory of Molecular Biology, Cambridge, UK.
Leila MureşanCambridge Advanced Imaging Centre, University of Cambridge, UK.
Yorgo ModisDepartment of Medicine, University of Cambridge, MRC Laboratory of Molecular Biology, UK.
MRC Laboratory of Molecular Biology · GBUniversity of Cambridge · GB

Funding

The structural basis of nucleic acid recognition by Toll-like receptorsR01GM102869 · NIGMS · YALE UNIVERSITY · PI MODIS, YORGO · 2012 to 2015
$1.1M
Biotechnology and Biological Sciences Research Council (BBSRC) 101908/Z/13/ZMedical Research Council MC_EX_MR/K015680/1Medical Research Council MC_U105184326NIGMS NIH HHS R01 GM102869Wellcome Trust 101908Wellcome Trust 101908/Z/13/Z
6 · The paper itself

Abstract

Double-stranded RNA (dsRNA) is a potent proinflammatory signature of viral infection and is sensed primarily by RIG-I-like receptors (RLRs). Oligomerization of RLRs following binding to cytosolic dsRNA activates and nucleates self-assembly of the mitochondrial antiviral-signaling protein (MAVS). In the current signaling model, the caspase recruitment domains of MAVS form helical fibrils that self-propagate like prions to promote signaling complex assembly. However, there is no conclusive evidence that MAVS forms fibrils in cells or with the transmembrane anchor present. We show here with super-resolution light microscopy that MAVS activation by dsRNA induces mitochondrial membrane remodeling. Quantitative image analysis at imaging resolutions as high as 32 nm shows that in the cellular context, MAVS signaling complexes and the fibrils within them are smaller than 80 nm. The transmembrane domain of MAVS is required for its membrane remodeling, interferon signaling, and proapoptotic activities. We conclude that membrane tethering of MAVS restrains its polymerization and contributes to mitochondrial remodeling and apoptosis upon dsRNA sensing.

Indexed as

3T3 CellsAdaptor Proteins, Signal TransducingAnimalsCell DeathCytosolFibroblastsInterferon-betaInterferon-Induced Helicase, IFIH1Membrane Transport ProteinsMiceMice, KnockoutMicroscopyMitochondrial MembranesMitochondrial Precursor Protein Import Complex ProteinsProtein DomainsReceptors, Cell SurfaceAdaptor Proteins, Signal TransducingIfih1 protein, mouseInterferon-betaInterferon-Induced Helicase, IFIH1MAVS protein, mouseMembrane Transport ProteinsMitochondrial Precursor Protein Import Complex ProteinsReceptors, Cell SurfaceRNA, Double-StrandedTomm20 protein, mousecell deathinnate immunitypathogen-associated molecular patternsignal transductionSTORM

Identifiers

PMID30715798
PMCPMC6513760
OpenAlexW2906303142

What OpenQuestion holds

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Registered trials

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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.