Cited by 451Muscle Physiology and DisordersGenomics and Rare DiseasesCellular transport and secretion

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Mutations in amphiphysin 2 (BIN1) disrupt interaction with dynamin 2 and cause autosomal recessive centronuclear myopathy

Nicot, Anne-Sophie, Toussaint, Anne, Tosch, Valérie, Kretz, Christine, Wallgren-Pettersson, Carina, Iwarsson, Erik, Kingston, Helen, Garnier, Jean-Marie, Biancalana, Valérie, Oldfors, Anders, Mandel, Jean-Louis, Laporte, Jocelyn·2007·Nature Genetics

DOI 10.1038/ng2086

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Abstract

Centronuclear myopathies are characterized by muscle weakness and abnormal centralization of nuclei in muscle fibers not secondary to regeneration. The severe neonatal X-linked form (myotubular myopathy) is due to mutations in the phosphoinositide phosphatase myotubularin (MTM1), whereas mutations in dynamin 2 (DNM2) have been found in some autosomal dominant cases. By direct sequencing of functional candidate genes, we identified homozygous mutations in amphiphysin 2 (BIN1) in three families with autosomal recessive inheritance. Two missense mutations affecting the BAR (Bin1/amphiphysin/RVS167) domain disrupt its membrane tubulation properties in transfected cells, and a partial truncation of the C-terminal SH3 domain abrogates the interaction with DNM2 and its recruitment to the membrane tubules. Our results suggest that mutations in BIN1 cause centronuclear myopathy by interfering with remodeling of T tubules and/or endocytic membranes, and that the functional interaction between BIN1 and DNM2 is necessary for normal muscle function and positioning of nuclei.

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Authors: Nicot, A.-S., Toussaint, A., Tosch, V., Kretz, C., Wallgren-Pettersson, C., Iwarsson, E., Kingston, H., Garnier, J.-M., Biancalana, V., Oldfors, A., Mandel, J.-L., & Laporte, J.
Affiliations: Centre National de la Recherche Scientifique (FR)
Karolinska University Hospital (SE)
Laboratoire de Génétique Médicale (FR)
Sahlgrenska University Hospital (SE)
Corresponding author: Laporte, Jocelyn
ORCID: Nicot, Anne-Sophie
Kretz, Christine
Iwarsson, Erik
Garnier, Jean-Marie
Biancalana, Valérie
Oldfors, Anders
Mandel, Jean-Louis
Laporte, Jocelyn
Venue: Nature Genetics
Publisher: Springer Science and Business Media LLC
Published: 2007-08-05
Volume: 39
Issue: 9
Pages: 1134-1139
ISSN: 1061-4036 (ISSN-L)
1546-1718
DOI: 10.1038/ng2086
OpenAlex: W2053365501
Cited by: 434
References: 33
Citations by year: 2026: 9 · 2025: 17 · 2024: 22 · 2023: 19 · 2022: 39 · 2021: 19 · 2020: 26 · 2019: 20 · 2018: 26 · 2017: 21 · 2016: 21 · 2015: 20 · 2014: 28 · 2013: 26 · 2012: 27
FWCI: 8.73
Type: journal article
Language: en
Open access: closed
Licence: www.springer.com/tdm (tdm)
Locations: Nature Genetics (publishedVersion)
PubMed (publishedVersion)
HAL (submittedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Genomics and Rare Diseases
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
Keywords: BIN1, dynamin 2, centronuclear myopathy, autosomal recessive inheritance, missense mutations, BAR domain, SH3 domain, protein-protein interaction, myotubular myopathy
MeSH terms: Amino Acid Sequence, Animals, Base Sequence, Binding Sites, Cell Line, Cell Nucleus, Chlorocebus aethiops, Female, Genes, Recessive, Haplotypes, Humans, Male, Molecular Sequence Data, Muscular Diseases, Mutation, Nerve Tissue Proteins, Protein Binding, Transfection, Sequence Homology, Amino Acid, Microscopy, Confocal, COS Cells, Polymorphism, Single Nucleotide, Dynamin II, Green Fluorescent Proteins, Mice

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Mutations in amphiphysin 2 (BIN1) disrupt interaction with dynamin 2 and cause autosomal recessive centronuclear myopathy

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