Evidence map›Paper›PMID 37155854›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2023

ATG5 selectively engages virus-tethered BST2/tetherin in an LC3C-associated pathway.

Delphine Judith, Margaux Versapuech, Fabienne Bejjani, Marjory Palaric, Pauline Verlhac, Aurelia Kuster, Leslie Lepont, Sarah Gallois-Montbrun, Katy Janvier, Clarisse Berlioz-Torrent

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
2.3field-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

14 citing papers in PubMed, 16 citations in OpenAlex.

  1. Review
  2. Review
  3. Autophagy andFrontiers in cellular and infection microbiology · 2026
    Review
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Neddylation modification stabilizes LC3B by antagonizing its ubiquitin-mediated degradation and promoting autophagy in skin.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  10. Article
  11. Article
  12. Somatic BrafAngiogenesis · 2024
    Article
  13. Article
  14. Review
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

10 authors at 1 institution in 1 country.

Delphine JudithUniversité Paris Cité, Institut Cochin, INSERM, CNRS, F-75014 Paris, France.ORCID 0000-0003-2098-4812
Margaux VersapuechUniversité Paris Cité, Institut Cochin, INSERM, CNRS, F-75014 Paris, France.
Fabienne BejjaniUniversité Paris Cité, Institut Cochin, INSERM, CNRS, F-75014 Paris, France.
Marjory PalaricUniversité Paris Cité, Institut Cochin, INSERM, CNRS, F-75014 Paris, France.
Pauline VerlhacUniversité Paris Cité, Institut Cochin, INSERM, CNRS, F-75014 Paris, France.
Aurelia KusterUniversité Paris Cité, Institut Cochin, INSERM, CNRS, F-75014 Paris, France.
Leslie LepontUniversité Paris Cité, Institut Cochin, INSERM, CNRS, F-75014 Paris, France.
Sarah Gallois-MontbrunUniversité Paris Cité, Institut Cochin, INSERM, CNRS, F-75014 Paris, France.ORCID 0000-0002-7870-1814
Katy JanvierUniversité Paris Cité, Institut Cochin, INSERM, CNRS, F-75014 Paris, France.ORCID 0000-0002-3105-4736
Clarisse Berlioz-TorrentUniversité Paris Cité, Institut Cochin, INSERM, CNRS, F-75014 Paris, France.ORCID 0000-0002-5782-8154
Centre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Bone marrow stromal antigen 2 (BST2)/tetherin is a restriction factor that reduces HIV-1 dissemination by tethering virus at the cell surface. BST2 also acts as a sensor of HIV-1 budding, establishing a cellular antiviral state. The HIV-1 Vpu protein antagonizes BST2 antiviral functions via multiple mechanisms, including the subversion of an LC3C-associated pathway, a key cell intrinsic antimicrobial mechanism. Here, we describe the first step of this viral-induced LC3C-associated process. This process is initiated at the plasma membrane through the recognition and internalization of virus-tethered BST2 by ATG5, an autophagy protein. ATG5 and BST2 assemble as a complex, independently of the viral protein Vpu and ahead of the recruitment of the ATG protein LC3C. The conjugation of ATG5 with ATG12 is dispensable for this interaction. ATG5 recognizes cysteine-linked homodimerized BST2 and specifically engages phosphorylated BST2 tethering viruses at the plasma membrane, in an LC3C-associated pathway. We also found that this LC3C-associated pathway is used by Vpu to attenuate the inflammatory responses mediated by virion retention. Overall, we highlight that by targeting BST2 tethering viruses, ATG5 acts as a signaling scaffold to trigger an LC3C-associated pathway induced by HIV-1 infection.

Indexed as

Bone Marrow Stromal Antigen 2VirusesAntiviral AgentsAutophagy-Related Protein 5Cell MembraneGPI-Linked ProteinsHuman Immunodeficiency Virus ProteinsHumansMicrotubule-Associated ProteinsViral ProteinsViral Regulatory and Accessory ProteinsAntiviral AgentsATG5 protein, humanAutophagy-Related Protein 5Bone Marrow Stromal Antigen 2GPI-Linked ProteinsHuman Immunodeficiency Virus ProteinsMAP1LC3C protein, humanMicrotubule-Associated ProteinsViral ProteinsViral Regulatory and Accessory ProteinsATG5BST2/tetherinHIV-1LC3-associated pathwaynon-canonical autophagy

Identifiers

PMID37155854
PMCPMC10193943
OpenAlexW4375954763

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.