ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2008
Identification of a motif in the acetylcholine receptor beta subunit whose phosphorylation regulates rapsyn association and postsynaptic receptor localization.
Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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40 citing papers in PubMed, 66 citations in OpenAlex.
- Review
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- Calcitriol ameliorates motor deficits and prolongs survival of Chrne-deficient mouse, a model for congenital myasthenic syndrome, by inducing Rspo2.Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2024Article
- The role of Rapsyn in neuromuscular junction and congenital myasthenic syndrome.Biomolecules & biomedicine · 2023Review
- Clinical and Pathologic Features of Congenital Myasthenic Syndromes Caused by 35 Genes-A Comprehensive Review.International journal of molecular sciences · 2023Review
- NMJ-related diseases beyond the congenital myasthenic syndromes.Frontiers in cell and developmental biology · 2023Review
- Speculation on How RIC-3 and Other Chaperones Facilitate α7 Nicotinic Receptor Folding and Assembly.Molecules (Basel, Switzerland) · 2022Review
- Anisotropic scaffolds for peripheral nerve and spinal cord regeneration.Bioactive materials · 2021Review
- Creating stem cell-derived neuromuscular junctions in vitro.Muscle & nerve · 2021Review
- Autoantibody of NRIP, a novel AChR-interacting protein, plays a detrimental role in myasthenia gravis.Journal of cachexia, sarcopenia and muscle · 2021Article
- An Inside Job: Molecular Determinants for Postsynaptic Localization of Nicotinic Acetylcholine Receptors.Molecules (Basel, Switzerland) · 2021Review
- CTGF/CCN2 facilitates LRP4-mediated formation of the embryonic neuromuscular junction.EMBO reports · 2020Article
- The MX-Helix of Muscle nAChR Subunits Regulates Receptor Assembly and Surface Trafficking.Frontiers in molecular neuroscience · 2020Article
- The Neuromuscular Junction in Health and Disease: Molecular Mechanisms Governing Synaptic Formation and Homeostasis.Frontiers in molecular neuroscience · 2020Review
- Muscle-Specific Kinase Myasthenia Gravis.Frontiers in immunology · 2020Review
- Current Status of Therapeutic Approaches against Peripheral Nerve Injuries: A Detailed Story from Injury to Recovery.International journal of biological sciences · 2020Review
- Vezatin is required for the maturation of the neuromuscular synapse.Molecular biology of the cell · 2019Article
- Effects of aging and Parkinson's disease on motor unit remodeling: influence of resistance exercise training.Journal of applied physiology (Bethesda, Md. : 1985) · 2018Article
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
At the neuromuscular junction, the acetylcholine receptor (AChR) is specifically clustered in the postsynaptic membrane via interactions with rapsyn and other scaffolding proteins. However, it remains unclear where these proteins bind on the AChR and how the interactions are regulated. Here, we define a phosphorylation-dependent binding site on the receptor that mediates agrin-induced clustering. Using chimeric proteins in which CD4 is fused to the large intracellular loop of each of the AChR subunits we found that agrin induced clustering of only chimeras containing the beta subunit loop. By making deletions in the beta loop we defined a 20 amino-acid sequence that is sufficient for clustering. The sequence contains a conserved tyrosine (Y390) whose phosphorylation is induced by agrin and whose mutation abolished clustering of beta loop chimeras and their ability to inhibit agrin-induced clustering of the endogenous AChR. Phosphorylation of the AChR beta subunit is correlated with increased rapsyn/AChR binding, suggesting that the effect of betaY390 phosphorylation on clustering is mediated by rapsyn. Indeed, we found that rapsyn associated with CD4-beta loop chimeras in a phosphorylation-dependent manner, and that agrin increased the ratio of rapsyn binding to wild type AChR but not to AChR-beta(3F/3F), which lacks beta loop tyrosine phosphorylation sites. Together, these findings suggest that agrin-induced phosphorylation of the beta subunit motif increases the stoichiometry of rapsyn binding to the AChR, thereby helping to stably cluster the receptor and anchor it at high density in the postsynaptic membrane.
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