The cell polarity protein Vangl2 in the muscle shapes the neuromuscular synapse by binding to and regulating the tyrosine kinase MuSK
| dc.rights.license | open | en_US |
| hal.structure.identifier | Centre de recherche en Myologie – U974 SU-INSERM | |
| dc.contributor.author | BOEX, Myriam | |
| hal.structure.identifier | Centre de recherche en Myologie – U974 SU-INSERM | |
| dc.contributor.author | COTTIN, Steve | |
| hal.structure.identifier | Centre de recherche en Myologie – U974 SU-INSERM | |
| dc.contributor.author | HALLIEZ, Marius | |
| hal.structure.identifier | Centre de recherche en Myologie – U974 SU-INSERM | |
| dc.contributor.author | BAUCHE, Stephanie | |
| hal.structure.identifier | Centre de recherche en Myologie – U974 SU-INSERM | |
| dc.contributor.author | BUON, Celine | |
| hal.structure.identifier | Neurocentre Magendie : Physiopathologie de la Plasticité Neuronale [U1215 Inserm - UB] | |
| dc.contributor.author | SANS, Nathalie | |
| hal.structure.identifier | Neurocentre Magendie : Physiopathologie de la Plasticité Neuronale [U1215 Inserm - UB] | |
| dc.contributor.author | MONTCOUQUIOL, Mireille | |
| hal.structure.identifier | Institut des Sciences du Vivant Frédéric JOLIOT [JOLIOT] | |
| dc.contributor.author | MOLGO, Jordi | |
| hal.structure.identifier | Institut des Sciences du Vivant Frédéric JOLIOT [JOLIOT] | |
| dc.contributor.author | AMAR, Muriel | |
| hal.structure.identifier | Centre de recherche en Myologie – U974 SU-INSERM | |
| dc.contributor.author | FERRY, Arnaud | |
| hal.structure.identifier | Phénotypage du petit animal [UMS28] | |
| dc.contributor.author | LEMAITRE, Megane | |
| hal.structure.identifier | Centre de recherche en Myologie – U974 SU-INSERM | |
| dc.contributor.author | ROUCHE, Andree | |
| hal.structure.identifier | Institut du Cerveau = Paris Brain Institute [ICM] | |
| dc.contributor.author | LANGUI, Dominique | |
| hal.structure.identifier | Institut du Cerveau = Paris Brain Institute [ICM] | |
| dc.contributor.author | BASKARAN, Asha | |
| hal.structure.identifier | Centre de recherche en Myologie – U974 SU-INSERM | |
| dc.contributor.author | FONTAINE, Bertrand | |
| hal.structure.identifier | Centre de recherche en Myologie – U974 SU-INSERM | |
| dc.contributor.author | MESSEANT, Julien | |
| hal.structure.identifier | Centre de recherche en Myologie – U974 SU-INSERM | |
| dc.contributor.author | STROCHLIC, Laure | |
| dc.date.accessioned | 2023-05-15T12:31:46Z | |
| dc.date.available | 2023-05-15T12:31:46Z | |
| dc.date.issued | 2022-05-17 | |
| dc.identifier.issn | 1945-0877 | en_US |
| dc.identifier.uri | https://oskar-bordeaux.fr/handle/20.500.12278/182142 | |
| dc.description.abstractEn | The development of the neuromuscular junction (NMJ) requires dynamic trans-synaptic coordination orchestrated by secreted factors, including Wnt family morphogens. To investigate how these synaptic cues in NMJ development are transduced, particularly in the regulation of acetylcholine receptor (AChR) accumulation in the postsynaptic membrane, we explored the function of Van Gogh-like protein 2 (Vangl2), a core component of Wnt planar cell polarity signaling. We found that conditional, muscle-specific ablation of Vangl2 in mice reproduced the NMJ differentiation defects seen in mice with global Vangl2 deletion. These alterations persisted into adulthood and led to NMJ disassembly, impaired neurotransmission, and deficits in motor function. Vangl2 and the muscle-specific receptor tyrosine kinase MuSK were functionally associated in Wnt signaling in the muscle. Vangl2 bound to and promoted the signaling activity of MuSK in response to Wnt11. The loss of Vangl2 impaired RhoA activation in cultured mouse myotubes and caused dispersed, rather than clustered, organization of AChRs at the postsynaptic or muscle cell side of NMJs in vivo. Our results identify Vangl2 as a key player of the core complex of molecules shaping neuromuscular synapses and thus shed light on the molecular mechanisms underlying NMJ assembly. Copyright © 2022 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. | |
| dc.language.iso | EN | en_US |
| dc.subject.en | Animals | |
| dc.subject.en | Cell Polarity | |
| dc.subject.en | Fatty Acids | |
| dc.subject.en | Monounsaturated | |
| dc.subject.en | Mice | |
| dc.subject.en | Muscle Fibers | |
| dc.subject.en | Skeletal / metabolism | |
| dc.subject.en | Nerve Tissue Proteins / metabolism | |
| dc.subject.en | Protein-Tyrosine Kinases | |
| dc.subject.en | Receptors | |
| dc.subject.en | Cholinergic / genetics Receptors | |
| dc.subject.en | Cholinergic / metabolism | |
| dc.subject.en | Synapses / genetics | |
| dc.subject.en | Synapses / metabolism | |
| dc.title.en | The cell polarity protein Vangl2 in the muscle shapes the neuromuscular synapse by binding to and regulating the tyrosine kinase MuSK | |
| dc.title.alternative | Sci Signal | en_US |
| dc.type | Article de revue | en_US |
| dc.identifier.doi | 10.1126/scisignal.abg4982 | en_US |
| dc.subject.hal | Sciences du Vivant [q-bio]/Neurosciences [q-bio.NC] | en_US |
| dc.identifier.pubmed | 35580169 | en_US |
| bordeaux.journal | Science Signaling | en_US |
| bordeaux.volume | 15 | en_US |
| bordeaux.hal.laboratories | Neurocentre Magendie - U1215 | en_US |
| bordeaux.issue | 734 | en_US |
| bordeaux.institution | Université de Bordeaux | en_US |
| bordeaux.institution | INSERM | en_US |
| bordeaux.team | Polarité planaire et plasticité | en_US |
| bordeaux.peerReviewed | oui | en_US |
| bordeaux.inpress | non | en_US |
| hal.export | false | |
| dc.rights.cc | Pas de Licence CC | en_US |
| bordeaux.COinS | ctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=Science%20Signaling&rft.date=2022-05-17&rft.volume=15&rft.issue=734&rft.eissn=1945-0877&rft.issn=1945-0877&rft.au=BOEX,%20Myriam&COTTIN,%20Steve&HALLIEZ,%20Marius&BAUCHE,%20Stephanie&BUON,%20Celine&rft.genre=article |
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