Evidence map›Paper›PMID 38858388›Full record

ArticleNature communications2024

Wnt-Ror-Dvl signalling and the dystrophin complex organize planar-polarized membrane compartments in C. elegans muscles.

Alice Peysson, Noura Zariohi, Marie Gendrel, Amandine Chambert-Loir, Noémie Frébault, Elise Cheynet, Olga Andrini, Thomas Boulin

Abstract read
In one paragraph

Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing 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

6 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Constitutive sodium permeability in aProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  5. Review
  6. Review
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

8 authors.

Alice Peysson *Université Claude Bernard Lyon 1, CNRS UMR 5284, INSERM U1314, MeLiS, Lyon, 69008, France.
Noura Zariohi *Université Claude Bernard Lyon 1, CNRS UMR 5284, INSERM U1314, MeLiS, Lyon, 69008, France.
Marie GendrelInstitut de Biologie de l'Ecole Normale Supérieure (IBENS), Ecole Normale Supérieure, CNRS, INSERM, Université Paris Sciences et Lettres Research University, Paris, 75005, France.ORCID http://orcid.org/0000-0002-0991-0479
Amandine Chambert-LoirUniversité Claude Bernard Lyon 1, CNRS UMR 5284, INSERM U1314, MeLiS, Lyon, 69008, France.
Noémie FrébaultUniversité Claude Bernard Lyon 1, CNRS UMR 5284, INSERM U1314, MeLiS, Lyon, 69008, France.
Elise CheynetUniversité Claude Bernard Lyon 1, CNRS UMR 5284, INSERM U1314, MeLiS, Lyon, 69008, France.
Olga AndriniUniversité Claude Bernard Lyon 1, CNRS UMR 5284, INSERM U1314, MeLiS, Lyon, 69008, France.ORCID http://orcid.org/0000-0001-7659-4771
Thomas BoulinUniversité Claude Bernard Lyon 1, CNRS UMR 5284, INSERM U1314, MeLiS, Lyon, 69008, France. thomas.boulin@univ-lyon1.fr.ORCID http://orcid.org/0000-0002-1734-1915

Funding

Enhancing and expanding the CGC Strain CollectionP40OD010440 · OD · UNIVERSITY OF MINNESOTA · PI Aric L Daul, Ann E. Rougvie · 2012 to 2026
$7.5M
AFM-Téléthon (French Muscular Dystrophy Association) MyoNeurALPAgence Nationale de la Recherche (French National Research Agency) DYSCOEC | EU Framework Programme for Research and Innovation H2020 | H2020 Priority Excellent Science | H2020 European Research Council (H2020 Excellent Science - European Research Council) KelegansNIH HHS P40 OD010440
6 · The paper itself

Abstract

Cell polarity mechanisms allow the formation of specialized membrane domains with unique protein compositions, signalling properties, and functional characteristics. By analyzing the localization of potassium channels and proteins belonging to the dystrophin-associated protein complex, we reveal the existence of distinct planar-polarized membrane compartments at the surface of C. elegans muscle cells. We find that muscle polarity is controlled by a non-canonical Wnt signalling cascade involving the ligand EGL-20/Wnt, the receptor CAM-1/Ror, and the intracellular effector DSH-1/Dishevelled. Interestingly, classical planar cell polarity proteins are not required for this process. Using time-resolved protein degradation, we demonstrate that -while it is essentially in place by the end of embryogenesis- muscle polarity is a dynamic state, requiring continued presence of DSH-1 throughout post-embryonic life. Our results reveal the unsuspected complexity of the C. elegans muscle membrane and establish a genetically tractable model system to study cellular polarity and membrane compartmentalization in vivo.

Indexed as

Caenorhabditis elegansCaenorhabditis elegans ProteinsCell PolarityDystrophinMusclesWnt Signaling PathwayAnimalsCell MembraneDishevelled ProteinsDystrophin-Associated Protein ComplexReceptor Tyrosine Kinase-like Orphan ReceptorsSignal TransductionWnt ProteinsCaenorhabditis elegans ProteinsCAM-1 protein, C elegansDishevelled ProteinsDystrophinDystrophin-Associated Protein ComplexEgl-20 protein, C elegansReceptor Tyrosine Kinase-like Orphan ReceptorsWnt Proteins

Identifiers

PMID38858388
PMCPMC11164867

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Registered trials

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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.