Evidence map›Paper›PMID 38377988›Full record

ArticleStructure (London, England : 1993)2024

Insertases scramble lipids: Molecular simulations of MTCH2.

Ladislav Bartoš, Anant K Menon, Robert Vácha

Open access · hybridAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
11.4field-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

28 citing papers in PubMed, 38 citations in OpenAlex.

  1. Article
  2. Article
  3. Structural evolution of the MTCH family of mitochondrial insertases.bioRxiv : the preprint server for biology · 2026
    Article
  4. Article
  5. Article
  6. Bridging Scales: Coarse-Grained Protein Models in Computational Biology.Advances in experimental medicine and biology · 2026
    Review
  7. Article
  8. Opsins are Phospholipid Scramblases in All Domains of Life.bioRxiv : the preprint server for biology · 2025
    Article
  9. Review
  10. Martini 3 Limitations in Phospholipid Flip-Flop.Journal of chemical theory and computation · 2025
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Lipid Scrambling Pathways in the Sec61 Translocon Complex.Journal of the American Chemical Society · 2025
    Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors at 2 institutions in 2 countries.

Ladislav BartošCEITEC - Central European Institute of Technology, Masaryk University, Kamenice 5, 625 00 Brno, Czech Republic; National Centre for Biomolecular Research, Faculty of Science, Masaryk University, Kamenice 5, 625 00 Brno, Czech Republic.
Anant K MenonDepartment of Biochemistry, Weill Cornell Medical College, New York, NY 10065, USA.
Robert VáchaCEITEC - Central European Institute of Technology, Masaryk University, Kamenice 5, 625 00 Brno, Czech Republic; National Centre for Biomolecular Research, Faculty of Science, Masaryk University, Kamenice 5, 625 00 Brno, Czech Republic; Department of Condensed Matter Physics, Faculty of Science, Masaryk University, Kotlářská 2, 611 37 Brno, Czech Republic. Electronic address: robert.vacha@muni.cz.
Central European Institute of Technology · CZCornell University · US

Funding

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 R21 NS119779
6 · The paper itself

Abstract

Scramblases play a pivotal role in facilitating bidirectional lipid transport across cell membranes, thereby influencing lipid metabolism, membrane homeostasis, and cellular signaling. MTCH2, a mitochondrial outer membrane protein insertase, has a membrane-spanning hydrophilic groove resembling those that form the lipid transit pathway in known scramblases. Employing both coarse-grained and atomistic molecular dynamics simulations, we show that MTCH2 significantly reduces the free energy barrier for lipid movement along the groove and therefore can indeed function as a scramblase. Notably, the scrambling rate of MTCH2 in silico is similar to that of voltage-dependent anion channel (VDAC), a recently discovered scramblase of the outer mitochondrial membrane, suggesting a potential complementary physiological role for these mitochondrial proteins. Finally, our findings suggest that other insertases which possess a hydrophilic path across the membrane like MTCH2, can also function as scramblases.

Indexed as

LipidsMolecular Dynamics SimulationCell MembraneLipidsflip-flop ratefree energy barrierhydrophilic grooveinsertasemembrane defectmolecular dynamicsscramblase

Identifiers

PMID38377988
PMCPMC11001264
OpenAlexW4391934091

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.