Evidence map›Paper›PMID 37983294›Full record

ArticlePLoS biology2023

ATG9A regulates the dissociation of recycling endosomes from microtubules to form liquid influenza A virus inclusions.

Sílvia Vale-Costa, Temitope Akhigbe Etibor, Daniela Brás, Ana Laura Sousa, Mariana Ferreira, Gabriel G Martins, Victor Hugo Mello, Maria João Amorim

Open access · goldAbstract read
In one paragraph

Article in PLoS biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
3.6field-weighted citation impact, top 6% 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

15 citing papers in PubMed, 17 citations in OpenAlex.

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  9. Progress on multifunctional transmembrane protein ATG9A.Cell communication and signaling : CCS · 2025
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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 2 institutions in 1 country.

Sílvia Vale-CostaCell Biology of Viral Infection Lab (CBV), Instituto Gulbenkian de Ciência (IGC)-Fundação Calouste Gulbenkian, Oeiras, Portugal.
Temitope Akhigbe EtiborCell Biology of Viral Infection Lab (CBV), Instituto Gulbenkian de Ciência (IGC)-Fundação Calouste Gulbenkian, Oeiras, Portugal.
Daniela BrásCell Biology of Viral Infection Lab (CBV), Instituto Gulbenkian de Ciência (IGC)-Fundação Calouste Gulbenkian, Oeiras, Portugal.
Ana Laura SousaElectron Microscopy Facility (EMF), Instituto Gulbenkian de Ciência (IGC)-Fundação Calouste Gulbenkian, Oeiras, Portugal.
Mariana FerreiraAdvanced Imaging Facility (AIF), Instituto Gulbenkian de Ciência (IGC)-Fundação Calouste Gulbenkian, Oeiras, Portugal.
Gabriel G MartinsAdvanced Imaging Facility (AIF), Instituto Gulbenkian de Ciência (IGC)-Fundação Calouste Gulbenkian, Oeiras, Portugal.
Victor Hugo MelloLiving Physics, Instituto Gulbenkian de Ciência (IGC)-Fundação Calouste Gulbenkian, Oeiras, Portugal.
Maria João AmorimCell Biology of Viral Infection Lab (CBV), Instituto Gulbenkian de Ciência (IGC)-Fundação Calouste Gulbenkian, Oeiras, Portugal.ORCID 0000-0002-4129-6659
Calouste Gulbenkian Foundation · PTUniversidade Católica Portuguesa · PT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

It is now established that many viruses that threaten public health establish condensates via phase transitions to complete their lifecycles, and knowledge on such processes may offer new strategies for antiviral therapy. In the case of influenza A virus (IAV), liquid condensates known as viral inclusions, concentrate the 8 distinct viral ribonucleoproteins (vRNPs) that form IAV genome and are viewed as sites dedicated to the assembly of the 8-partite genomic complex. Despite not being delimited by host membranes, IAV liquid inclusions accumulate host membranes inside as a result of vRNP binding to the recycling endocytic marker Rab11a, a driver of the biogenesis of these structures. We lack molecular understanding on how Rab11a-recycling endosomes condensate specifically near the endoplasmic reticulum (ER) exit sites upon IAV infection. We show here that liquid viral inclusions interact with the ER to fuse, divide, and slide. We uncover that, contrary to previous indications, the reported reduction in recycling endocytic activity is a regulated process rather than a competition for cellular resources involving a novel role for the host factor ATG9A. In infection, ATG9A mediates the removal of Rab11a-recycling endosomes carrying vRNPs from microtubules. We observe that the recycling endocytic usage of microtubules is rescued when ATG9A is depleted, which prevents condensation of Rab11a endosomes near the ER. The failure to produce viral inclusions accumulates vRNPs in the cytosol and reduces genome assembly and the release of infectious virions. We propose that the ER supports the dynamics of liquid IAV inclusions, with ATG9A facilitating their formation. This work advances our understanding on how epidemic and pandemic influenza genomes are formed. It also reveals the plasticity of recycling endosomes to undergo condensation in response to infection, disclosing new roles for ATG9A beyond its classical involvement in autophagy.

Indexed as

Influenza A virusAutophagy-Related ProteinsEndoplasmic ReticulumEndosomesMembrane ProteinsMicrotubulesRibonucleoproteinsAutophagy-Related ProteinsMembrane ProteinsRibonucleoproteins

Identifiers

PMID37983294
PMCPMC10695400
OpenAlexW4388843797

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.