Evidence map›Paper›PMID 32471988›Full record

ArticleNature communications2020

Human ESCRT-III polymers assemble on positively curved membranes and induce helical membrane tube formation.

Aurélie Bertin, Nicola de Franceschi, Eugenio de la Mora, Sourav Maity, Maryam Alqabandi, Nolwen Miguet, Aurélie di Cicco, Wouter H Roos, Stéphanie Mangenot, Winfried Weissenhorn and 1 more

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 64 papers.

0numbers the graph read from it
0cells of the map it votes in
64citing papers in PubMed
9.9field-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

64 citing papers in PubMed, 129 citations in OpenAlex.

  1. Article
  2. Review
  3. Phosphatidylinositol diphosphate binding by ESCRT-III filaments.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  4. Article
  5. Membrane interaction of cyanobacterial and chloroplast ESCRT-III proteins.The Plant journal : for cell and molecular biology · 2026
    Review
  6. ESCRT-III function in membrane fission and repair.Nature reviews. Molecular cell biology · 2026
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. 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
  13. Review
  14. ESCRTing the RABs through conversion.Biochemical Society transactions · 2025
    Review
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Article

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

11 authors at 2 institutions in 2 countries.

Aurélie Bertin *Laboratoire Physico Chimie Curie, Institut Curie, PSL Research University, CNRS UMR168, 75005, Paris, France. aurelie.bertin@curie.fr.ORCID http://orcid.org/0000-0002-3400-6887
Nicola de Franceschi *Laboratoire Physico Chimie Curie, Institut Curie, PSL Research University, CNRS UMR168, 75005, Paris, France. N.deFranceschi@tudelft.nl.ORCID http://orcid.org/0000-0002-7221-613X
Eugenio de la MoraLaboratoire Physico Chimie Curie, Institut Curie, PSL Research University, CNRS UMR168, 75005, Paris, France.ORCID http://orcid.org/0000-0001-6945-7357
Sourav MaityMoleculaire Biofysica, Zernike Instituut, Rijksuniversiteit Groningen, Nijenborgh 4, 9747, AG Groningen, The Netherlands.
Maryam AlqabandiLaboratoire Physico Chimie Curie, Institut Curie, PSL Research University, CNRS UMR168, 75005, Paris, France.
Nolwen MiguetUniv. Grenoble Alpes, CEA, CNRS, Institut de Biologie Structurale (IBS), 71, avenue des Martyrs, 38000, Grenoble, France.
Aurélie di CiccoLaboratoire Physico Chimie Curie, Institut Curie, PSL Research University, CNRS UMR168, 75005, Paris, France.
Wouter H RoosMoleculaire Biofysica, Zernike Instituut, Rijksuniversiteit Groningen, Nijenborgh 4, 9747, AG Groningen, The Netherlands.
Stéphanie MangenotLaboratoire Physico Chimie Curie, Institut Curie, PSL Research University, CNRS UMR168, 75005, Paris, France.ORCID http://orcid.org/0000-0001-6470-0469
Winfried WeissenhornUniv. Grenoble Alpes, CEA, CNRS, Institut de Biologie Structurale (IBS), 71, avenue des Martyrs, 38000, Grenoble, France. winfried.weissenhorn@ibs.fr.ORCID http://orcid.org/0000-0001-5532-4959
Patricia BassereauLaboratoire Physico Chimie Curie, Institut Curie, PSL Research University, CNRS UMR168, 75005, Paris, France. patricia.bassereau@curie.fr.ORCID http://orcid.org/0000-0002-8544-6778
Centre National de la Recherche Scientifique · FRUniversity of Groningen · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Endosomal sorting complexes for transport-III (ESCRT-III) assemble in vivo onto membranes with negative Gaussian curvature. How membrane shape influences ESCRT-III polymerization and how ESCRT-III shapes membranes is yet unclear. Human core ESCRT-III proteins, CHMP4B, CHMP2A, CHMP2B and CHMP3 are used to address this issue in vitro by combining membrane nanotube pulling experiments, cryo-electron tomography and AFM. We show that CHMP4B filaments preferentially bind to flat membranes or to tubes with positive mean curvature. Both CHMP2B and CHMP2A/CHMP3 assemble on positively curved membrane tubes. Combinations of CHMP4B/CHMP2B and CHMP4B/CHMP2A/CHMP3 are recruited to the neck of pulled membrane tubes and reshape vesicles into helical "corkscrew-like" membrane tubes. Sub-tomogram averaging reveals that the ESCRT-III filaments assemble parallel and locally perpendicular to the tube axis, highlighting the mechanical stresses imposed by ESCRT-III. Our results underline the versatile membrane remodeling activity of ESCRT-III that may be a general feature required for cellular membrane remodeling processes.

Indexed as

Membranes, ArtificialStress, MechanicalATPases Associated with Diverse Cellular ActivitiesBiochemical PhenomenaCryoelectron MicroscopyEndosomal Sorting Complexes Required for TransportHumansNanotubesPolymerizationProtein BindingProtein MultimerizationVacuolar Proton-Translocating ATPasesATPases Associated with Diverse Cellular ActivitiesCHMP2A protein, humanCHMP2B protein, humanCHMP3 protein, humanCHMP4B protein, humanEndosomal Sorting Complexes Required for TransportMembranes, ArtificialVacuolar Proton-Translocating ATPasesVPS4A protein, human

Identifiers

PMID32471988
PMCPMC7260177
OpenAlexW3031605222

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.