Evidence map›Paper›PMID 38092770›Full record

ArticleNature communications2023

Molecular mechanism of phospholipid transport at the bacterial outer membrane interface.

Jiang Yeow, Min Luo, Shu-Sin Chng

Abstract 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 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing 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

16 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Advances in understanding Ton and Tol system motor proteins.Biochemical Society transactions · 2026
    Review
  8. Review
  9. Article
  10. Review
  11. Following phospholipid transfer through the OmpFProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  12. Lipid Trafficking in Diverse Bacteria.Accounts of chemical research · 2025
    Review
  13. Article
  14. Article
  15. The Mla system and its role in maintaining outer membrane barrier function inFrontiers in cellular and infection microbiology · 2024
    Article
  16. 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

3 authors.

Jiang YeowDepartment of Chemistry, Faculty of Science, National University of Singapore, Singapore, 117543, Singapore.ORCID 0000-0001-5384-7211
Min LuoDepartment of Biological Sciences, Faculty of Science, National University of Singapore, Singapore, 117558, Singapore.
Shu-Sin ChngDepartment of Chemistry, Faculty of Science, National University of Singapore, Singapore, 117543, Singapore. chmchngs@nus.edu.sg.ORCID 0000-0001-5466-7183

Funding

MOH | National Medical Research Council (NMRC) MOH-000145
6 · The paper itself

Abstract

The outer membrane (OM) of Gram-negative bacteria is an asymmetric lipid bilayer with outer leaflet lipopolysaccharides and inner leaflet phospholipids (PLs). This unique lipid asymmetry renders the OM impermeable to external insults, including antibiotics and bile salts. To maintain this barrier, the OmpC-Mla system removes mislocalized PLs from the OM outer leaflet, and transports them to the inner membrane (IM); in the first step, the OmpC-MlaA complex transfers PLs to the periplasmic chaperone MlaC, but mechanistic details are lacking. Here, we biochemically and structurally characterize the MlaA-MlaC transient complex. We map the interaction surfaces between MlaA and MlaC in Escherichia coli, and show that electrostatic interactions are important for MlaC recruitment to the OM. We further demonstrate that interactions with MlaC modulate conformational states in MlaA. Finally, we solve a 2.9-Å cryo-EM structure of a disulfide-trapped OmpC-MlaA-MlaC complex in nanodiscs, reinforcing the mechanism of MlaC recruitment, and highlighting membrane thinning as a plausible strategy for directing lipids for transport. Our work offers critical insights into retrograde PL transport by the OmpC-Mla system in maintaining OM lipid asymmetry.

Indexed as

Bacterial Outer MembraneEscherichia coli ProteinsBacterial Outer Membrane ProteinsBiological TransportCell MembraneEscherichia coliLipid BilayersLipopolysaccharidesMembrane LipidsPhospholipidsBacterial Outer Membrane ProteinsEscherichia coli ProteinsLipid BilayersLipopolysaccharidesMembrane LipidsPhospholipids

Identifiers

PMID38092770
PMCPMC10719372

What OpenQuestion holds

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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.