Evidence map›Paper›PMID 41571644›Full record

ArticleNature communications2026

A trans-synaptic IgLON adhesion molecular complex directly contacts and clusters a nicotinic receptor.

Morgane Mialon, Liubov Patrash, Laure Granger, Weinreb Alexis, Engin Özkan, Jean-Louis Bessereau, Berangere Pinan-Lucarre

Abstract read
In one paragraph

Article in Nature communications, 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. Postsynaptic Complexin Mediates Constitutive Exocytosis of Nicotinic Acetylcholine Receptor.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  2. Article
  3. A gene expression atlas of a juvenile nervous system.bioRxiv : the preprint server for biology · 2025
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors.

Morgane MialonUniversite Claude Bernard Lyon 1, MeLis, CNRS UMR5284, INSERM U1314, Faculte de Medecine et de Pharmacie, Lyon, France.
Liubov PatrashUniversite Claude Bernard Lyon 1, MeLis, CNRS UMR5284, INSERM U1314, Faculte de Medecine et de Pharmacie, Lyon, France.ORCID http://orcid.org/0009-0006-0284-1606
Laure GrangerUniversite Claude Bernard Lyon 1, MeLis, CNRS UMR5284, INSERM U1314, Faculte de Medecine et de Pharmacie, Lyon, France.
Weinreb AlexisDepartment of Genetics, Yale University School of Medicine, New Haven, CT, USA.
Engin ÖzkanDepartment of Biochemistry and Molecular Biology, University of Chicago, Chicago, IL, USA.ORCID http://orcid.org/0000-0002-0263-6729
Jean-Louis Bessereau *Universite Claude Bernard Lyon 1, MeLis, CNRS UMR5284, INSERM U1314, Faculte de Medecine et de Pharmacie, Lyon, France. jean-louis.bessereau@univ-lyon1.fr.ORCID http://orcid.org/0000-0002-3088-7621
Berangere Pinan-Lucarre *Universite Claude Bernard Lyon 1, MeLis, CNRS UMR5284, INSERM U1314, Faculte de Medecine et de Pharmacie, Lyon, France. berangere.pinan-lucarre@univ-lyon1.fr.ORCID http://orcid.org/0000-0002-6866-4714

Funding

Enhancing and expanding the CGC Strain CollectionP40OD010440 · OD · UNIVERSITY OF MINNESOTA · PI Aric L Daul, Ann E. Rougvie · 2012 to 2026
$7.5M
Mechanistic studies of molecular recognition and signaling of neuronal wiring receptorsR01NS139060 · NINDS · UNIVERSITY OF CHICAGO · PI Robert Arnulfo Carrillo, Engin Ozkan · 2024 to 2026
$1.5M
Agence Nationale de la Recherche (French National Research Agency) ANR-11-LABX-0042Agence Nationale de la Recherche (French National Research Agency) ANR-22CE16-0024-01EC | EU Framework Programme for Research and Innovation H2020 | H2020 Priority Excellent Science | H2020 European Research Council (H2020 Excellent Science - European Research Council) ERC_Adg C.NAPSE #695295Fondation pour la Recherche Médicale (Foundation for Medical Research in France) EQU202303016267Fondation pour la Recherche Médicale (Foundation for Medical Research in France) FRM-MND-202411019867NIH HHS P40 OD010440NINDS NIH HHS R01 NS139060
6 · The paper itself

Abstract

The clustering of neurotransmitter receptors at appropriate postsynaptic sites is essential for controlling synaptic transmission. While most known mechanisms involve receptor binding with cytoplasmic scaffolds, recent evidence highlights the importance of extracellular interactions that directly target receptors. Using Caenorhabditis elegans, we identified a trans-synaptic complex that involves RIG-5 and ZIG-8, two adhesion molecules of the immunoglobulin (Ig) superfamily and orthologous to Drosophila DIPs and Dprs, and mammalian IgLONs. Our results show that RIG-5 and ZIG-8 are anchored in the pre- and postsynaptic membranes, respectively, and interact in vivo via their first Ig domains. Furthermore, ZIG-8 directly binds a α7-like acetylcholine receptor (AChR), known as ACR-16, via a cis-interaction between its Ig2 domain and the base of the extracellular AChR domain. This study provides direct evidence that trans-synaptic IgLON interactions can organize neurochemical synapses and suggests that the IgLONs may directly interact with ionotropic receptors in the mammalian nervous system.

Indexed as

Caenorhabditis elegansCaenorhabditis elegans ProteinsReceptors, NicotinicSynapsesAnimalsImmunoglobulin DomainsImmunoglobulinsProtein BindingSynaptic TransmissionCaenorhabditis elegans ProteinsImmunoglobulinsReceptors, Nicotinic

Identifiers

PMID41571644
PMCPMC12881522

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.