N‐WASP is required for Amphiphysin‐2/BIN1‐dependent nuclear positioning and triad organization in skeletal muscle and is involved in the pathophysiology of centronuclear myopathy
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Mutations in amphiphysin-2/BIN1, dynamin 2, and myotubularin are associated with centronuclear myopathy (CNM), a muscle disorder characterized by myofibers with atypical central nuclear positioning and abnormal triads. Mis-splicing of amphiphysin-2/BIN1 is also associated with myotonic dystrophy that shares histopathological hallmarks with CNM. How amphiphysin-2 orchestrates nuclear positioning and triad organization and how CNM-associated mutations lead to muscle dysfunction remains elusive. We find that N-WASP interacts with amphiphysin-2 in myofibers and that this interaction and N-WASP distribution are disrupted by amphiphysin-2 CNM mutations. We establish that N-WASP functions downstream of amphiphysin-2 to drive peripheral nuclear positioning and triad organization during myofiber formation. Peripheral nuclear positioning requires microtubule/Map7/Kif5b-dependent distribution of nuclei along the myofiber and is driven by actin and nesprins. In adult myofibers, N-WASP and amphiphysin-2 are only involved in the maintenance of triad organization but not in the maintenance of peripheral nuclear positioning. Importantly, we confirmed that N-WASP distribution is disrupted in CNM and myotonic dystrophy patients. Our results support a role for N-WASP in amphiphysin-2-dependent nuclear positioning and triad organization and in CNM and myotonic dystrophy pathophysiology.
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The BIN1 SH3 domain can interact with proteins including c-Abl, N-WASP, actin, myosin, and Tau, suggesting involvement of the cytoskeleton in BIN1 function.
“In addition to proteins involved in endocytosis, the BIN1 SH3 domain can interact with a number of other proteins including the tyrosine kinase c-Abl, the actin nucleation-promoting factor N-WASP, actin, myosin, and Tau, suggesting the involvement of the cytoskeleton in BIN1 function [18–21].”
From Predominant expression of Alzheimer’s disease-associated BIN1 in mature oligodendrocytes and localization to white matter tracts (2016) · cites this paper as [20]
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Caveolae and Bin1 form ring-shaped platforms for T-tubule initiation
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Self-citationPhospholamban overexpression in mice causes a centronuclear myopathy-like phenotype
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Nuclear Mechanotransduction in Skeletal Muscle
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Self-citationNesprin-1: novel regulator of striated muscle nuclear positioning and mechanotransduction
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Interrogating RNA and protein spatial subcellular distribution in smFISH data with DypFISH
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Self-citationNuclear defects in skeletal muscle from a Dynamin 2-linked centronuclear myopathy mouse model
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BIN1 and Alzheimer’s disease: the tau connection
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Self-citationNuclear movement in multinucleated cells
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Amphiphysin-2 (BIN1) functions and defects in cardiac and skeletal muscle
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Ma2/d promotes myonuclear positioning and association with the sarcoplasmic reticulum
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Self-citationBIN1 regulates actin-membrane interactions during IRSp53-dependent filopodia formation
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Self-citationCellular and Genomic Features of Muscle Differentiation from Isogenic Fibroblasts and Myoblasts
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MAP7 drives EMT and cisplatin resistance in ovarian cancer via wnt/β-catenin signaling
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BIN1 gene replacement reverses BIN1-related centronuclear myopathy
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Self-citationMechanosensitive clathrin platforms anchor desmin intermediate filaments in skeletal musclePreprint
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Self-citationDynamics of triadin, a muscle-specific triad protein, within sarcoplasmic reticulum subdomains
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Identification of CaVβ1 Isoforms Required for Neuromuscular Junction Formation and Maintenance
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Self-citationSH3KBP1 promotes skeletal myofiber formation and functionality through ER/SR architecture integrity
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Unravelling the role of mitochondrial dysfunction in core myopathies
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SH3KBP1 scaffolds endoplasmic reticulum and controls skeletal myofibers architecture and integrityPreprint
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Self-citationCongenital Myopathies and Related Disorders
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Self-citation
- Authors
- Falcone, S., Roman, W., Hnia, K., Gache, V., Didier, N., Lainé, J., Auradé, F., Marty, I., Nishino, I., Charlet‐Berguerand, N., Romero, N. B., Marazzi, G., Sassoon, D., Laporte, J., & Gomes, E. R.
- Affiliations
- Inserm (FR)
- Centre National de la Recherche Scientifique (FR)
- Institut de Myologie (FR)
- National Center of Neurology and Psychiatry (JP)
- University of Lisbon (PT)
- Corresponding author
- Falcone, Sestina
- Gomes, Edgar R
- ORCID
- Venue
- EMBO Molecular Medicine
- Published
- 2014-09-29
- Volume
- 6
- Issue
- 11
- Pages
- 1455-1475
- ISSN
- 1757-4676 (ISSN-L)
- 1757-4684
- PMC
- PMC4237471
- OpenAlex
- W2122457898
- Cited by
- 116
- References
- 63
- Citations by year
- 2026: 2 · 2025: 13 · 2024: 10 · 2023: 5 · 2022: 7 · 2021: 16 · 2020: 9 · 2019: 9 · 2018: 16 · 2017: 12 · 2016: 10 · 2015: 5 · 2014: 2
- FWCI
- 3.97
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- EMBO Molecular Medicine (publishedVersion, other-oa)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- HAL (submittedVersion, cc-by)
- HAL (submittedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
- Portuguese National Funding Agency for Science, Research and Technology (RCAAP Project by FCT) (submittedVersion, other-oa)
- univOAK (4 institutions : Université de Strasbourg, Université de Haute Alsace, INSA Strasbourg, Bibliothèque Nationale et Universitaire de Strasbourg) (submittedVersion, cc-by)
- Funders
- Muscular Dystrophy Association
- INSERM Avenir programme
- European Research Council
- EMBO installation
- Agence Nationale de la Recherche
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Genomics and Rare Diseases
- Keywords
- N-WASP, BIN1, centronuclear myopathy, myotonic dystrophy, nuclear positioning, skeletal muscle, myofiber formation, microtubules, KIF5B, nesprins, actin, dynamin 2, myotubularin, protein-protein interaction
- MeSH terms
- Adult, Humans, Nuclear Proteins, Muscle, Skeletal, Muscle Fibers, Skeletal, Myopathies, Structural, Congenital, Tumor Suppressor Proteins, Adaptor Proteins, Signal Transducing, Mutant Proteins, Wiskott-Aldrich Syndrome Protein, Neuronal
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