Evidence map›Paper›PMID 37759741›Full record

ArticleBiomolecules2023

Role of Lipids and Divalent Cations in Membrane Fusion Mediated by the Heptad Repeat Domain 1 of Mitofusin.

Anaïs Vlieghe, Kristina Niort, Hugo Fumat, Jean-Michel Guigner, Mickaël M Cohen, David Tareste

Open access · goldAbstract read
In one paragraph

Article in Biomolecules, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.9field-weighted citation impact, top 24% 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

3 citing papers in PubMed, 6 citations in OpenAlex.

  1. PMF proteins mediate mitochondrial fusion in Arabidopsis.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Review
  3. Mfn2-dependent fusion pathway of PE-enriched micron-sized vesicles.Proceedings of the National Academy of Sciences of the United States of America · 2024
    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

6 authors at 2 institutions in 1 country.

Anaïs VliegheUniversité Paris Cité, Institute of Psychiatry and Neuroscience of Paris (IPNP), Inserm UMR-S 1266, Team Membrane Traffic in Healthy & Diseased Brain, 75014 Paris, France.ORCID 0000-0003-1655-115X
Kristina NiortUniversité Paris Cité, Institute of Psychiatry and Neuroscience of Paris (IPNP), Inserm UMR-S 1266, Team Membrane Traffic in Healthy & Diseased Brain, 75014 Paris, France.
Hugo FumatUniversité Paris Cité, Institute of Psychiatry and Neuroscience of Paris (IPNP), Inserm UMR-S 1266, Team Membrane Traffic in Healthy & Diseased Brain, 75014 Paris, France.
Jean-Michel GuignerSorbonne Université, Institut de Minéralogie, de Physique des Matériaux et de Cosmochimie (IMPMC), CNRS UMR 7590, MNHN, IRD UR 206, 75005 Paris, France.
Mickaël M CohenSorbonne Université, Institut de Biologie Physico-Chimique (IBPC), CNRS UMR 8226, Laboratoire de Biologie Moléculaire et Cellulaire des Eucaryotes, 75005 Paris, France.ORCID 0000-0002-1372-680X
David TaresteUniversité Paris Cité, Institute of Psychiatry and Neuroscience of Paris (IPNP), Inserm UMR-S 1266, Team Membrane Traffic in Healthy & Diseased Brain, 75014 Paris, France.ORCID 0000-0002-8744-7598
Inserm · FRCentre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mitochondria are highly dynamic organelles that constantly undergo fusion and fission events to maintain their shape, distribution and cellular function. Mitofusin 1 and 2 proteins are two dynamin-like GTPases involved in the fusion of outer mitochondrial membranes (OMM). Mitofusins are anchored to the OMM through their transmembrane domain and possess two heptad repeat domains (HR1 and HR2) in addition to their N-terminal GTPase domain. The HR1 domain was found to induce fusion via its amphipathic helix, which interacts with the lipid bilayer structure. The lipid composition of mitochondrial membranes can also impact fusion. However, the precise mode of action of lipids in mitochondrial fusion is not fully understood. In this study, we examined the role of the mitochondrial lipids phosphatidylethanolamine (PE), cardiolipin (CL) and phosphatidic acid (PA) in membrane fusion induced by the HR1 domain, both in the presence and absence of divalent cations (Ca

Indexed as

Membrane FusionMitochondriaCations, DivalentGTP PhosphohydrolasesLipidsMitochondrial MembranesCations, DivalentGTP PhosphohydrolasesLipidsamphipathic helixdivalent cationsfusionlipid packing defectsmembranemitochondriaMitofusin

Identifiers

PMID37759741
PMCPMC10527301
OpenAlexW4386417754

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.