Evidence map›Paper›PMID 38065946›Full record

ArticleNature communications2023

Phospholipids are imported into mitochondria by VDAC, a dimeric beta barrel scramblase.

Helene Jahn, Ladislav Bartoš, Grace I Dearden, Jeremy S Dittman, Joost C M Holthuis, Robert Vácha, Anant K Menon

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
8.8field-weighted citation impact, top 2% 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

40 citing papers in PubMed, 57 citations in OpenAlex.

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  12. Article
  13. Opsins are Phospholipid Scramblases in All Domains of Life.bioRxiv : the preprint server for biology · 2025
    Article
  14. Martini 3 Limitations in Phospholipid Flip-Flop.Journal of chemical theory and computation · 2025
    Article
  15. Article
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  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

7 authors at 3 institutions in 3 countries.

Helene JahnDepartment of Biochemistry, Weill Cornell Medical College, New York, NY, 10065, USA.
Ladislav BartošCEITEC - Central European Institute of Technology, Masaryk University, Kamenice 5, 62500, Brno, Czech Republic.
Grace I DeardenDepartment of Biochemistry, Weill Cornell Medical College, New York, NY, 10065, USA.
Jeremy S DittmanDepartment of Biochemistry, Weill Cornell Medical College, New York, NY, 10065, USA.ORCID 0000-0002-3850-9078
Joost C M HolthuisDepartment of Molecular Cell Biology, University of Osnabrück, Osnabrück, 49076, Germany.ORCID 0000-0001-8912-1586
Robert VáchaCEITEC - Central European Institute of Technology, Masaryk University, Kamenice 5, 62500, Brno, Czech Republic. robert.vacha@muni.cz.ORCID 0000-0001-7610-658X
Anant K MenonDepartment of Biochemistry, Weill Cornell Medical College, New York, NY, 10065, USA. akm2003@med.cornell.edu.ORCID 0000-0001-6924-2698
Cornell University · USCentral European Institute of Technology · CZOsnabrück University · DE

Funding

Analysis of Synaptic Protein DynamicsR01NS116747 · NINDS · WEILL MEDICAL COLL OF CORNELL UNIV · PI Jeremy Samuel Dittman · 2020 to 2026
$2.6M
A mitochondrial phospholipid scramblase for cardiolipin biosynthesisR21NS119779 · NINDS · WEILL MEDICAL COLL OF CORNELL UNIV · PI MENON, ANANT K · 2020 to 2020
$463k
NINDS NIH HHS R01 NS116747NINDS NIH HHS R21 NS119779
6 · The paper itself

Abstract

Mitochondria are double-membrane-bounded organelles that depend critically on phospholipids supplied by the endoplasmic reticulum. These lipids must cross the outer membrane to support mitochondrial function, but how they do this is unclear. We identify the Voltage Dependent Anion Channel (VDAC), an abundant outer membrane protein, as a scramblase-type lipid transporter that catalyzes lipid entry. On reconstitution into membrane vesicles, dimers of human VDAC1 and VDAC2 catalyze rapid transbilayer translocation of phospholipids by a mechanism that is unrelated to their channel activity. Coarse-grained molecular dynamics simulations of VDAC1 reveal that lipid scrambling occurs at a specific dimer interface where polar residues induce large water defects and bilayer thinning. The rate of phospholipid import into yeast mitochondria is an order of magnitude lower in the absence of VDAC homologs, indicating that VDACs provide the main pathway for lipid entry. Thus, VDAC isoforms, members of a superfamily of beta barrel proteins, moonlight as a class of phospholipid scramblases - distinct from alpha-helical scramblase proteins - that act to import lipids into mitochondria.

Indexed as

PhospholipidsVoltage-Dependent Anion Channel 1HumansMitochondriaSaccharomyces cerevisiaeVoltage-Dependent Anion ChannelsPhospholipidsVoltage-Dependent Anion Channel 1Voltage-Dependent Anion Channels

Identifiers

PMID38065946
PMCPMC10709637
OpenAlexW4389482913

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.