Evidence map›Paper›PMID 30989108›Full record

ArticleScience advances2019

VPS4 triggers constriction and cleavage of ESCRT-III helical filaments.

Sourav Maity, Christophe Caillat, Nolwenn Miguet, Guidenn Sulbaran, Gregory Effantin, Guy Schoehn, Wouter H Roos, Winfried Weissenhorn

Open access · goldAbstract read
In one paragraph

Article in Science advances, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.

0numbers the graph read from it
0cells of the map it votes in
56citing papers in PubMed
8.5field-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

56 citing papers in PubMed, 110 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. ESCRT-III function in membrane fission and repair.Nature reviews. Molecular cell biology · 2026
    Review
  5. Membrane interaction of cyanobacterial and chloroplast ESCRT-III proteins.The Plant journal : for cell and molecular biology · 2026
    Review
  6. Article
  7. Article
  8. The bacterial ESCRT-III PspA rods thin lipid tubules and increase membrane curvature through helix α0 interactions.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
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  12. Article
  13. Review
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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 2 countries.

Sourav MaityMoleculaire Biofysica, Zernike Instituut, Rijksuniversiteit Groningen, Nijenborgh 4, 9747 AG Groningen, Netherlands.ORCID 0000-0003-1614-0879
Christophe CaillatInstitut de Biologie Structurale (IBS), Univ. Grenoble Alpes, CEA, CNRS, 71 Avenue des Martyrs, 38000 Grenoble, France.
Nolwenn MiguetInstitut de Biologie Structurale (IBS), Univ. Grenoble Alpes, CEA, CNRS, 71 Avenue des Martyrs, 38000 Grenoble, France.
Guidenn SulbaranInstitut de Biologie Structurale (IBS), Univ. Grenoble Alpes, CEA, CNRS, 71 Avenue des Martyrs, 38000 Grenoble, France.
Gregory EffantinInstitut de Biologie Structurale (IBS), Univ. Grenoble Alpes, CEA, CNRS, 71 Avenue des Martyrs, 38000 Grenoble, France.
Guy SchoehnInstitut de Biologie Structurale (IBS), Univ. Grenoble Alpes, CEA, CNRS, 71 Avenue des Martyrs, 38000 Grenoble, France.ORCID 0000-0002-1459-3201
Wouter H RoosMoleculaire Biofysica, Zernike Instituut, Rijksuniversiteit Groningen, Nijenborgh 4, 9747 AG Groningen, Netherlands.
Winfried WeissenhornInstitut de Biologie Structurale (IBS), Univ. Grenoble Alpes, CEA, CNRS, 71 Avenue des Martyrs, 38000 Grenoble, France.ORCID 0000-0001-5532-4959
Centre National de la Recherche Scientifique · FRUniversity of Groningen · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Many cellular processes such as endosomal vesicle budding, virus budding, and cytokinesis require extensive membrane remodeling by the endosomal sorting complex required for transport III (ESCRT-III). ESCRT-III protein family members form spirals with variable diameters in vitro and in vivo inside tubular membrane structures, which need to be constricted to proceed to membrane fission. Here, we show, using high-speed atomic force microscopy and electron microscopy, that the AAA-type adenosine triphosphatase VPS4 constricts and cleaves ESCRT-III CHMP2A-CHMP3 helical filaments in vitro. Constriction starts asymmetrically and progressively decreases the diameter of CHMP2A-CHMP3 tubular structure, thereby coiling up the CHMP2A-CHMP3 filaments into dome-like end caps. Our results demonstrate that VPS4 actively constricts ESCRT-III filaments and cleaves them before their complete disassembly. We propose that the formation of ESCRT-III dome-like end caps by VPS4 within a membrane neck structure constricts the membrane to set the stage for membrane fission.

Indexed as

Adenosine TriphosphateEndosomal Sorting Complexes Required for TransportHydrolysisMicroscopy, Atomic ForceModels, MolecularProtein ConformationProtein MultimerizationVacuolar Proton-Translocating ATPasesAdenosine TriphosphateEndosomal Sorting Complexes Required for TransportVacuolar Proton-Translocating ATPases

Identifiers

PMID30989108
PMCPMC6457934
OpenAlexW2939170806

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.