Evidence map›Paper›PMID 42285089›Full record

ArticleCell2026

Mechanism of lipid transfer by bridge-like protein VPS13A and the scramblase XK.

Bodan Hu, Daniel Álvarez, Cristian Rocha-Roa, Valentin Guyard, Dazhi Li, Yara Ahmed, Xinbo Wang, Pietro De Camilli, Stefano Vanni, Karin M Reinisch

Abstract read
In one paragraph

Article in Cell, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. 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

10 authors.

Bodan HuDepartment of Cell Biology, Yale University School of Medicine, New Haven, CT, USA.
Daniel ÁlvarezDepartment of Biology, University of Fribourg, 1700 Fribourg, Switzerland; Department of Engineering, Universidad Loyola Andalucía, Avenida de las Universidades, Seville, Spain.
Cristian Rocha-RoaDepartment of Biology, University of Fribourg, 1700 Fribourg, Switzerland.
Valentin GuyardDepartment of Biology, University of Fribourg, 1700 Fribourg, Switzerland.
Dazhi LiDepartment of Cell Biology, Yale University School of Medicine, New Haven, CT, USA.
Yara AhmedDepartment of Biology, University of Fribourg, 1700 Fribourg, Switzerland.
Xinbo WangDepartment of Cell Biology, Yale University School of Medicine, New Haven, CT, USA; Department of Neuroscience, Yale University School of Medicine, New Haven, CT, USA; Howard Hughes Medical Institute, Yale University School of Medicine, New Haven, CT, USA; Program in Cellular Neuroscience, Neurodegeneration, and Repair, Yale University School of Medicine, New Haven, CT, USA.
Pietro De CamilliDepartment of Cell Biology, Yale University School of Medicine, New Haven, CT, USA; Department of Neuroscience, Yale University School of Medicine, New Haven, CT, USA; Howard Hughes Medical Institute, Yale University School of Medicine, New Haven, CT, USA; Program in Cellular Neuroscience, Neurodegeneration, and Repair, Yale University School of Medicine, New Haven, CT, USA.
Stefano VanniDepartment of Biology, University of Fribourg, 1700 Fribourg, Switzerland; Swiss National Center for Competence in Research Bio-Inspired Materials, University of Fribourg, 1700 Fribourg, Switzerland. Electronic address: stefano.vanni@unifr.ch.
Karin M ReinischDepartment of Cell Biology, Yale University School of Medicine, New Haven, CT, USA. Electronic address: karin.reinisch@yale.edu.

Funding

Yale/NIDA Neuroproteomics Research CenterP30DA018343 · NIDA · YALE UNIVERSITY · PI ANGUS C. NAIRN, Kenneth Robert WILLIAMS · 2004 to 2026
$37.1M
Molecular Basis for Membrane Lipid HomeostasisR35GM131715 · NIGMS · YALE UNIVERSITY · PI KARIN M REINISCH · 2019 to 2026
$6.5M
NIDA NIH HHS P30 DA018343NIGMS NIH HHS R35 GM131715
6 · The paper itself

Abstract

In eukaryotes, bridge-like lipid-transfer proteins (BLTPs) are central in mediating vesicle-independent lipid transfer between organelles. BLTPs span the cytosolic space between organelles at contact sites, featuring hydrophobic channels for lipids to travel between membranes. How BLTPs cooperate with partner proteins to orchestrate lipid delivery remains a mystery. Here, we used cryo-electron microscopy to visualize a complex comprising the prototypical BLTP VPS13A and the plasma membrane-localized scramblase XK at near-atomic resolution. VPS13A interacts with XK via its pleckstrin homology domain, priming VPS13A's bridge-like lipid-transfer domain to deliver lipids directly to the cytosolic leaflet of the acceptor membrane. In molecular dynamics simulations, this arrangement allows for robust lipid transfer. Newly delivered lipids can then be equilibrated between leaflets of the membrane bilayer by the scramblase, allowing for membrane growth. Mechanistic insights regarding lipid delivery by VPS13A are directly applicable to all VPS13 proteins and, more broadly, to all BLTP family members.

Indexed as

Phospholipid Transfer ProteinsVesicular Transport ProteinsCell MembraneChaetomiumCryoelectron MicroscopyHumansMolecular Dynamics SimulationSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsPhospholipid Transfer ProteinsSaccharomyces cerevisiae ProteinsVesicular Transport ProteinsVPS13 protein, S cerevisiaebridge-like lipid-transfer proteincryo-EMlipid transfermembrane contact sitesmolecular dynamics simulationsscramblaseVPS13XK

Identifiers

PMID42285089
PMCPMC13267863

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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.