Evidence map›Paper›PMID 33832485›Full record

ArticleBMC biology2021

The ESCRT-III isoforms CHMP2A and CHMP2B display different effects on membranes upon polymerization.

Maryam Alqabandi, Nicola de Franceschi, Sourav Maity, Nolwenn Miguet, Marta Bally, Wouter H Roos, Winfried Weissenhorn, Patricia Bassereau, Stéphanie Mangenot

Open access · goldAbstract read
In one paragraph

Article in BMC biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.5field-weighted citation impact, top 11% 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

23 citing papers in PubMed, 34 citations in OpenAlex.

  1. Phosphatidylinositol diphosphate binding by ESCRT-III filaments.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Review
  11. Review
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. 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

9 authors at 3 institutions in 3 countries.

Maryam Alqabandi *Laboratoire Physico Chimie Curie, Institut Curie, Université PSL, Sorbonne Université, CNRS UMR168, 75005, Paris, France.
Nicola de Franceschi *Laboratoire Physico Chimie Curie, Institut Curie, Université PSL, Sorbonne Université, CNRS UMR168, 75005, Paris, France.
Sourav MaityMoleculaire Biofysica, Zernike Instituut, Rijksuniversiteit Groningen, Nijenborgh 4, 9747 AG, Groningen, The Netherlands.
Nolwenn MiguetUniv. Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale (IBS), 38000, Grenoble, France.
Marta BallyUmeå University, Department of Clinical Microbiology & Wallenberg Centre for Molecular Medicine, 90185, Umeå, Sweden.
Wouter H RoosMoleculaire Biofysica, Zernike Instituut, Rijksuniversiteit Groningen, Nijenborgh 4, 9747 AG, Groningen, The Netherlands.
Winfried Weissenhorn *Univ. Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale (IBS), 38000, Grenoble, France.
Patricia Bassereau *Laboratoire Physico Chimie Curie, Institut Curie, Université PSL, Sorbonne Université, CNRS UMR168, 75005, Paris, France.
Stéphanie Mangenot *Laboratoire Physico Chimie Curie, Institut Curie, Université PSL, Sorbonne Université, CNRS UMR168, 75005, Paris, France. stephanie.mangenot@curie.fr.ORCID 0000-0001-6470-0469
Centre National de la Recherche Scientifique · FRUniversity of Groningen · NLUmeå University · SE

Funding

agence nationale de la recherche ANR-11- 798 LABX0038Agence nationale de la recherche ANR-10-IDEX-0001-02Agence Nationale de la Recherche ANR-10-INBS-05-02Agence Nationale de la Recherche ANR-10-INSB-04Agence Nationale de la Recherche ANR-14-CE09-0003-01Agence Nationale de la Recherche ANR-17-EURE-0003fondation pour la recherche médicale ALTF 818-2016H2020 European Research Council MSCA No. 751715H2020 Marie Skłodowska-Curie Actions INTERACT 751404ISBG UMS 3518 CNRS-CEA-UGA-EMBL
6 · The paper itself

Abstract

backgroundESCRT-III proteins are involved in many membrane remodeling processes including multivesicular body biogenesis as first discovered in yeast. In humans, ESCRT-III CHMP2 exists as two isoforms, CHMP2A and CHMP2B, but their physical characteristics have not been compared yet.

resultsHere, we use a combination of techniques on biomimetic systems and purified proteins to study their affinity and effects on membranes. We establish that CHMP2B binding is enhanced in the presence of PI(4,5)P2 lipids. In contrast, CHMP2A does not display lipid specificity and requires CHMP3 for binding significantly to membranes. On the micrometer scale and at moderate bulk concentrations, CHMP2B forms a reticular structure on membranes whereas CHMP2A (+CHMP3) binds homogeneously. Thus, CHMP2A and CHMP2B unexpectedly induce different mechanical effects to membranes: CHMP2B strongly rigidifies them while CHMP2A (+CHMP3) has no significant effect.

conclusionsWe therefore conclude that CHMP2B and CHMP2A exhibit different mechanical properties and might thus contribute differently to the diverse ESCRT-III-catalyzed membrane remodeling processes.

Indexed as

Cell MembraneEndosomal Sorting Complexes Required for TransportPolymerizationCHMP2A protein, humanCHMP2B protein, humanEndosomal Sorting Complexes Required for TransportAtomic force microscopy (AFM)Bottom up approachEndosomal sorting complexes Required for Transport (ESCRT)Giant unilamellar vesicles (GUV)Lipid-protein interactionsMechanical propertiesMembraneMicropipetteReconstituted system

Identifiers

PMID33832485
PMCPMC8033747
OpenAlexW3152208772

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.