Evidence map›Paper›PMID 40527982›Full record

ArticleCommunications biology2025

Membrane lipid composition modulates the organization of VDAC1, a mitochondrial gatekeeper.

Elodie Lafargue, Jean-Pierre Duneau, Nicolas Buzhinsky, Pamela Ornelas, Alexandre Ortega, Varun Ravishankar, James Sturgis, Ignacio Casuso, Lucie Bergdoll

Abstract read
In one paragraph

Article in Communications biology, 2025. 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
–field-weighted citation impact
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.

  1. Article
  2. Article
  3. Elliptical β-barrel deformation underlies gating in VDAC1.Protein science : a publication of the Protein Society · 2026
    Article
  4. Review
  5. Review
  6. Article
  7. Article
  8. Mitochondrial medicine in obesity: a scoping review.Open medicine (Warsaw, Poland) · 2026
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Approaches to Organelle Spacing at Membrane Contact Sites.Contact (Thousand Oaks (Ventura County, Calif.))
    Article
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.

Elodie Lafargue *Turing Centre for Living System, Aix-Marseille Université, U1325 INSERM, DyNaMo, Marseille, France.
Jean-Pierre Duneau *Laboratoire d'Ingénierie des Systèmes Macromoléculaires, CNRS - Aix Marseille Université, Marseille, France.
Nicolas BuzhinskyTuring Centre for Living System, Aix-Marseille Université, U1325 INSERM, DyNaMo, Marseille, France.ORCID http://orcid.org/0000-0003-2488-5707
Pamela OrnelasDepartment of Structural Biology, Max Planck Institute of Biophysics, Frankfurt, Germany.ORCID http://orcid.org/0000-0002-7015-9215
Alexandre OrtegaTuring Centre for Living System, Aix-Marseille Université, U1325 INSERM, DyNaMo, Marseille, France.
Varun RavishankarLaboratoire d'Ingénierie des Systèmes Macromoléculaires, CNRS - Aix Marseille Université, Marseille, France.
James SturgisLaboratoire d'Ingénierie des Systèmes Macromoléculaires, CNRS - Aix Marseille Université, Marseille, France.ORCID http://orcid.org/0000-0001-5125-7699
Ignacio CasusoTuring Centre for Living System, Aix-Marseille Université, U1325 INSERM, DyNaMo, Marseille, France. ignacio.casuso@inserm.fr.ORCID http://orcid.org/0000-0001-7192-0136
Lucie BergdollLaboratoire d'Ingénierie des Systèmes Macromoléculaires, CNRS - Aix Marseille Université, Marseille, France. lbergdoll@imm.cnrs.fr.ORCID http://orcid.org/0000-0001-6068-238X

Funding

Agence Nationale de la Recherche (French National Research Agency) ANR-19-CE11-0024Agence Nationale de la Recherche (French National Research Agency) ANR-21-CE42-0031Aix-Marseille Université (Aix-Marseille University) AMX-21-PEP-022
6 · The paper itself

Abstract

VDACs, the most abundant proteins in the outer mitochondrial membrane (MOM), are crucial for mitochondrial physiology. VDAC regulate metabolite and ion exchange, modulate calcium homeostasis, and play roles in numerous cellular events such as apoptosis, mitochondrial DNA (mtDNA) release, and different diseases. Mitochondrial function is closely tied to VDAC oligomerization, influencing key processes like mtDNA release and apoptosis, but the molecular drivers of this oligomerization remain unclear. In this study, we investigate the effects of three major MOM lipids on VDAC assemblies using atomic force microscopy and molecular dynamics simulations. Our results show that phosphatidylethanolamine and cholesterol regulate VDAC assembly, with the formation of stable lipid-protein organization of various size and compaction. Deviations from physiological lipid content disrupted native-like VDAC assemblies, highlighting the importance of lipid environment in VDAC organization. These findings underscore how lipid heterogeneity and changes in membranes influence VDAC function.

Indexed as

Membrane LipidsMitochondriaMitochondrial MembranesVoltage-Dependent Anion Channel 1CholesterolHumansMicroscopy, Atomic ForceMolecular Dynamics SimulationPhosphatidylethanolaminesCholesterolMembrane LipidsphosphatidylethanolaminePhosphatidylethanolaminesVDAC1 protein, humanVoltage-Dependent Anion Channel 1

Identifiers

PMID40527982
PMCPMC12174345

What OpenQuestion holds

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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.