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The cell polarity protein Vangl2 in the muscle shapes the neuromuscular synapse by binding to and regulating the tyrosine kinase MuSK

dc.rights.licenseopenen_US
hal.structure.identifierCentre de recherche en Myologie – U974 SU-INSERM
dc.contributor.authorBOEX, Myriam
hal.structure.identifierCentre de recherche en Myologie – U974 SU-INSERM
dc.contributor.authorCOTTIN, Steve
hal.structure.identifierCentre de recherche en Myologie – U974 SU-INSERM
dc.contributor.authorHALLIEZ, Marius
hal.structure.identifierCentre de recherche en Myologie – U974 SU-INSERM
dc.contributor.authorBAUCHE, Stephanie
hal.structure.identifierCentre de recherche en Myologie – U974 SU-INSERM
dc.contributor.authorBUON, Celine
hal.structure.identifierNeurocentre Magendie : Physiopathologie de la Plasticité Neuronale [U1215 Inserm - UB]
dc.contributor.authorSANS, Nathalie
hal.structure.identifierNeurocentre Magendie : Physiopathologie de la Plasticité Neuronale [U1215 Inserm - UB]
dc.contributor.authorMONTCOUQUIOL, Mireille
hal.structure.identifierInstitut des Sciences du Vivant Frédéric JOLIOT [JOLIOT]
dc.contributor.authorMOLGO, Jordi
hal.structure.identifierInstitut des Sciences du Vivant Frédéric JOLIOT [JOLIOT]
dc.contributor.authorAMAR, Muriel
hal.structure.identifierCentre de recherche en Myologie – U974 SU-INSERM
dc.contributor.authorFERRY, Arnaud
hal.structure.identifierPhénotypage du petit animal [UMS28]
dc.contributor.authorLEMAITRE, Megane
hal.structure.identifierCentre de recherche en Myologie – U974 SU-INSERM
dc.contributor.authorROUCHE, Andree
hal.structure.identifierInstitut du Cerveau = Paris Brain Institute [ICM]
dc.contributor.authorLANGUI, Dominique
hal.structure.identifierInstitut du Cerveau = Paris Brain Institute [ICM]
dc.contributor.authorBASKARAN, Asha
hal.structure.identifierCentre de recherche en Myologie – U974 SU-INSERM
dc.contributor.authorFONTAINE, Bertrand
hal.structure.identifierCentre de recherche en Myologie – U974 SU-INSERM
dc.contributor.authorMESSEANT, Julien
hal.structure.identifierCentre de recherche en Myologie – U974 SU-INSERM
dc.contributor.authorSTROCHLIC, Laure
dc.date.accessioned2023-05-15T12:31:46Z
dc.date.available2023-05-15T12:31:46Z
dc.date.issued2022-05-17
dc.identifier.issn1945-0877en_US
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/182142
dc.description.abstractEnThe 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.isoENen_US
dc.subject.enAnimals
dc.subject.enCell Polarity
dc.subject.enFatty Acids
dc.subject.enMonounsaturated
dc.subject.enMice
dc.subject.enMuscle Fibers
dc.subject.enSkeletal / metabolism
dc.subject.enNerve Tissue Proteins / metabolism
dc.subject.enProtein-Tyrosine Kinases
dc.subject.enReceptors
dc.subject.enCholinergic / genetics Receptors
dc.subject.enCholinergic / metabolism
dc.subject.enSynapses / genetics
dc.subject.enSynapses / metabolism
dc.title.enThe cell polarity protein Vangl2 in the muscle shapes the neuromuscular synapse by binding to and regulating the tyrosine kinase MuSK
dc.title.alternativeSci Signalen_US
dc.typeArticle de revueen_US
dc.identifier.doi10.1126/scisignal.abg4982en_US
dc.subject.halSciences du Vivant [q-bio]/Neurosciences [q-bio.NC]en_US
dc.identifier.pubmed35580169en_US
bordeaux.journalScience Signalingen_US
bordeaux.volume15en_US
bordeaux.hal.laboratoriesNeurocentre Magendie - U1215en_US
bordeaux.issue734en_US
bordeaux.institutionUniversité de Bordeauxen_US
bordeaux.institutionINSERMen_US
bordeaux.teamPolarité planaire et plasticitéen_US
bordeaux.peerReviewedouien_US
bordeaux.inpressnonen_US
hal.exportfalse
dc.rights.ccPas de Licence CCen_US
bordeaux.COinSctx_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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