Evidence map›Paper›PMID 41564130›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2026

The molecular mechanism of lipid uptake by membrane-anchored bridge-like lipid transfer proteins.

Daniel Álvarez, Paige Chandran Blair, Cristian Rocha-Roa, Michael Davey, Elizabeth Conibear, Stefano Vanni

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2026. 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
–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

3 citing papers in PubMed.

  1. Article
  2. Article
  3. The molecular mechanism of lipid uptake by membrane-anchored bridge-like lipid transfer proteins.Proceedings of the National Academy of Sciences of the United States of America · 2026
    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.

Daniel ÁlvarezDepartment of Biology, University of Fribourg, Fribourg 1700, Switzerland.ORCID 0000-0002-8918-9916
Paige Chandran BlairDepartment of Cellular and Physiological Sciences, University of British Columbia, Vancouver, BC VH6 3N1, Canada.ORCID 0009-0009-8422-6253
Cristian Rocha-RoaDepartment of Biology, University of Fribourg, Fribourg 1700, Switzerland.ORCID 0000-0002-4602-6121
Michael DaveyCentre for Molecular Medicine and Therapeutics, British Columbia Children's Hospital Research Institute, University of British Columbia, Vancouver, BC V5Z 4H4, Canada.ORCID 0000-0002-1172-5934
Elizabeth ConibearCentre for Molecular Medicine and Therapeutics, British Columbia Children's Hospital Research Institute, University of British Columbia, Vancouver, BC V5Z 4H4, Canada.ORCID 0000-0001-5129-0499
Stefano VanniDepartment of Biology, University of Fribourg, Fribourg 1700, Switzerland.ORCID 0000-0003-2146-1140

Funding

Canada Foundation for Innovation (CFI) 39914Canadian Institutes of Health Research (CIHR) OGB-177941Canadian Institutes of Health Research (CIHR) PJT-180544Centro Svizzero di Calcolo Scientifico (CSCS) lp24Centro Svizzero di Calcolo Scientifico (CSCS) lp69Centro Svizzero di Calcolo Scientifico (CSCS) s1269EC | Horizon Europe | Excellent Science | HORIZON EUROPE European Research Council (ERC) 803952Margarita Salas program 2021-2023 funded by Ministerio de Universidades MU-21-UP2021-030-53773022Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung (SNF) CRSII5_189996
6 · The paper itself

Abstract

Lipid transport by bridge-like lipid transfer proteins (BLTPs) is emerging as a key process in lipid and cellular metabolism in both physiological and pathological conditions. However, the precise mechanism of lipid transport by BLTPs has remained elusive. Here, we use extensive all-atom molecular dynamics simulations to characterize the precise mechanism of lipid transfer into the BLTP hydrophobic cavity from donor membranes. For multiple BLTPs, we observe the ability to extract and solubilize lipids without lipid selectivity, and we identify membrane destabilization as a critical parameter to achieve effective lipid desorption. We rationally design a mutant BLTP with altered ability to destabilize lipid bilayers, and we show that this abolishes lipid desorption in silico and protein function in vivo. Taken together, our data provide an atomic-level description of the mechanism of lipid transport by BLTPs, ultimately suggesting alternative strategies to interfere with their activity.

Indexed as

Carrier ProteinsLipid BilayersLipid MetabolismBiological TransportCell MembraneHydrophobic and Hydrophilic InteractionsMolecular Dynamics SimulationCarrier ProteinsLipid Bilayerslipid transfer proteinlipid membraneslipid transportmembrane traffickingmolecular dynamicsorganelle

Identifiers

PMID41564130
PMCPMC12849699

What OpenQuestion holds

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LicenceCC BY-NC-ND
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.