Evidence map›Paper›PMID 42547564›Full record

ArticleThe EMBO journal2026

Membrane lipid composition and rapid endocytic retrieval modulate Wingless secretion.

Ines Alvarez-Rodrigo, David Willnow, Cyrille Alexandre, Claire Lebarbenchon, Annabel Borg, Heather Findlay, Maya Hoad Leftley, Ikram Arahouan, Yuguang Zhao, Florencia di Pietro and 6 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in The EMBO journal, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

16 authors.

Ines Alvarez-RodrigoThe Francis Crick Institute, London, UK. ines.alvarezrodrigo@crick.ac.uk.ORCID http://orcid.org/0000-0003-2181-5535
David WillnowThe Francis Crick Institute, London, UK.ORCID http://orcid.org/0000-0001-6220-3901
Cyrille AlexandreThe Francis Crick Institute, London, UK.
Claire LebarbenchonThe Francis Crick Institute, London, UK.ORCID http://orcid.org/0009-0004-3827-8179
Annabel BorgThe Francis Crick Institute, London, UK.ORCID http://orcid.org/0000-0003-2873-7226
Heather FindlayThe Francis Crick Institute, London, UK.
Maya Hoad LeftleyThe Francis Crick Institute, London, UK.ORCID http://orcid.org/0009-0004-9724-944X
Ikram ArahouanLIMES-Institute, Unit Development, Genetics and Molecular Physiology, Department for Molecular Developmental Biology, University of Bonn, Bonn, Germany.
Yuguang ZhaoDivision of Structural Biology, Wellcome Centre for Human Genetics, University of Oxford, Oxford, UK.
Florencia di PietroInstitut Curie, Université PSL, Sorbonne Université, CNRS UMR 3215, Inserm U934, Genetics and Developmental Biology, Paris, France.
Svend KjaerThe Francis Crick Institute, London, UK.
Paula BoothThe Francis Crick Institute, London, UK.
Reinhard BauerLIMES-Institute, Unit Development, Genetics and Molecular Physiology, Department for Molecular Developmental Biology, University of Bonn, Bonn, Germany.
E Yvonne JonesDivision of Structural Biology, Wellcome Centre for Human Genetics, University of Oxford, Oxford, UK.ORCID http://orcid.org/0000-0002-3834-1893
Yohanns BellaïcheInstitut Curie, Université PSL, Sorbonne Université, CNRS UMR 3215, Inserm U934, Genetics and Developmental Biology, Paris, France.ORCID http://orcid.org/0000-0003-1686-2943
Jean-Paul VincentThe Francis Crick Institute, London, UK. JP.Vincent@crick.ac.uk.ORCID http://orcid.org/0000-0003-2305-5744

Funding

Agence Nationale de la Recherche (ANR) TiMecaDiv 20CE13000801CNRS | Institut des sciences biologiques (INSB) UMR3215Deutsche Forschungsgemeinschaft (DFG) SFB 645Francis Crick Institute (FCI) FC001204Institut Curie (institut_curie) UMR3215-U934Institut National de la Santé et de la Recherche Médicale (Inserm) U934Wellcome Trust FC001204Wellcome Trust (WT) 214259/Z/18/Wellcome Trust (WT) 223133/Z/21/Z
6 · The paper itself

Abstract

The Wnt family ligands carry a lipid moiety that must be shielded from the aqueous environment. During secretion, this is achieved by the cargo receptor Wntless. The effect of acute endocytosis inhibition suggests that Wingless dissociates from Wntless at the apical plasma membrane but is prevented from being released extracellularly by rapid endocytosis. Super-resolution microscopy shows that Wingless then traffics, without Wntless, through specialized Rab7/Rab4-positive endosomes before basolateral release. In the absence of endocytosis, apical release is allowed, albeit in punctae. Similar punctae are formed upon abrogation of the ceramide synthase Schlank. We suggest that they represent insoluble aggregates since they are 'solubilized' by the lipid-binding protein Dally-like protein. Moreover, purified Wingless forms similar-looking structures that are solubilised by liposomes in vitro. These findings suggest that membrane lipid composition could modulate the stability of the Wingless-Wntless complex and/or the lipid bilayer's ability to accommodate the Wingless lipid. Together with rapid endocytosis, this ensures orderly transfer of Wingless from Wntless to the membrane, preventing aggregation, and promoting basolateral secretion.

Indexed as

Cell MembraneDrosophila ProteinsEndocytosisMembrane LipidsWnt1 ProteinAnimalsEndosomesProtein TransportDrosophila ProteinsMembrane Lipidswg protein, DrosophilaWnt1 Protein

Identifiers

PMID42547564
PMCPMC13534635

What OpenQuestion holds

Textmetadata
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.