Cited by 381Muscle Physiology and DisordersPI3K/AKT/mTOR signaling in cancerMuscle metabolism and nutrition

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Muscle inactivation of mTOR causes metabolic and dystrophin defects leading to severe myopathy

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Risson, Valérie, Mazelin, Laetitia, Roceri, Mila, Sanchez, Hervé, Moncollin, Vincent, Corneloup, Claudine, Richard-Bulteau, Hélène, Vignaud, Alban, Baas, Dominique, Defour, Aurélia, Freyssenet, Damien, Tanti, Jean-François, Le-Marchand-Brustel, Yannick, Ferrier, Bernard, Conjard-Duplany, Agnès, Romanino, Klaas, Bauché, Stéphanie, Hantaï, Daniel, Mueller, Matthias, Kozma, Sara C., Thomas, George, Rüegg, Markus A., Ferry, Arnaud, Pende, Mario, Bigard, Xavier, Koulmann, Nathalie, Schaeffer, Laurent, Gangloff, Yann-Gaël·2009·Journal of Cell Biology

DOI 10.1083/jcb.200903131PMC PMC2806319

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Abstract

Mammalian target of rapamycin (mTOR) is a key regulator of cell growth that associates with raptor and rictor to form the mTOR complex 1 (mTORC1) and mTORC2, respectively. Raptor is required for oxidative muscle integrity, whereas rictor is dispensable. In this study, we show that muscle-specific inactivation of mTOR leads to severe myopathy, resulting in premature death. mTOR-deficient muscles display metabolic changes similar to those observed in muscles lacking raptor, including impaired oxidative metabolism, altered mitochondrial regulation, and glycogen accumulation associated with protein kinase B/Akt hyperactivation. In addition, mTOR-deficient muscles exhibit increased basal glucose uptake, whereas whole body glucose homeostasis is essentially maintained. Importantly, loss of mTOR exacerbates the myopathic features in both slow oxidative and fast glycolytic muscles. Moreover, mTOR but not raptor and rictor deficiency leads to reduced muscle dystrophin content. We provide evidence that mTOR controls dystrophin transcription in a cell-autonomous, rapamycin-resistant, and kinase-independent manner. Collectively, our results demonstrate that mTOR acts mainly via mTORC1, whereas regulation of dystrophin is raptor and rictor independent.

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Authors: Risson, V., Mazelin, L., Roceri, M., Sanchez, H., Moncollin, V., Corneloup, C., Richard-Bulteau, H., Vignaud, A., Baas, D., Defour, A., Freyssenet, D., Tanti, J.-F., Le-Marchand-Brustel, Y., Ferrier, B., Conjard-Duplany, A., Romanino, K., Bauché, S., Hantaï, D., Mueller, M., Kozma, S. C., Thomas, G., Rüegg, M. A., Ferry, A., Pende, M., Bigard, X., Koulmann, N., Schaeffer, L., & Gangloff, Y.-G.
Affiliations: École Normale Supérieure de Lyon (FR)
Inserm (FR)
Service de Santé des Armées (FR)
Department of Human Factors, Research Center of the Health of the Military, La Tronche 38702, France 3
Université Pierre-et-Marie-Curie (FR)
Université de Lyon (FR)
Institut National de la Santé et de la Recherche Médicale, Unité 895, Centre Méditerranéen de Médecine Moléculaire, F-06204 Nice, France 6
Lyon 1 Université (FR)
Métabolomique et Maladies Métaboliques, Institut National de la Santé et de la Recherche Médicale, Unité 820, Faculté de Médecine R.T.H. Laennec, Université Claude Bernard Lyon 1, 69372 Lyon Cedex 08, France 8
University of Basel (CH)
Institut National de la Santé et de la Recherche Médicale, Université Pierre et Marie Curie, Unité Mixte de Recherche 975, Hôpital de la Salpêtrière, 75651 Paris Cedex 13, France 10
Novartis (Switzerland) (CH)
University of Cincinnati (US)
Corresponding author: Schaeffer, Laurent
Gangloff, Yann-Gaël
ORCID: Risson, Valérie
Mazelin, Laetitia
Moncollin, Vincent
Baas, Dominique
Defour, Aurélia
Freyssenet, Damien
Tanti, Jean-François
Bauché, Stéphanie
Mueller, Matthias
Thomas, George
Rüegg, Markus A.
Ferry, Arnaud
Pende, Mario
Bigard, Xavier
Schaeffer, Laurent
Gangloff, Yann-Gaël
Venue: Journal of Cell Biology
Publisher: Rockefeller University Press
Published: 2009-12-14
Volume: 187
Issue: 6
Pages: 859-874
ISSN: 0021-9525 (ISSN-L)
1540-8140
DOI: 10.1083/jcb.200903131
PMC: PMC2806319
OpenAlex: W2164316354
Cited by: 381
References: 52
Citations by year: 2026: 8 · 2025: 14 · 2024: 17 · 2023: 15 · 2022: 26 · 2021: 31 · 2020: 28 · 2019: 25 · 2018: 23 · 2017: 31 · 2016: 28 · 2015: 22 · 2014: 28 · 2013: 27 · 2012: 26
FWCI: 7.78
Type: journal article
Language: en
Open access: bronze
doi.org
Locations: The Journal of Cell Biology (publishedVersion)
PubMed Central (publishedVersion, cc-by-nc-sa)
PubMed (publishedVersion)
edoc (University of Basel) (acceptedVersion)
HAL (submittedVersion)
Dipòsit Digital de la Universitat de Barcelona (Universitat de Barcelona) (submittedVersion, cc-by)
Funders: Agence Nationale de la Recherche (ANR-06-BLAN-0354)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › PI3K/AKT/mTOR signaling in cancer
Health Sciences › Nursing › Nutrition and Dietetics › Muscle metabolism and nutrition
Keywords: mTOR, mTORC1, mTORC2, raptors, Rictor, muscle myopathies, dystrophin, oxidative metabolism, mitochondrial regulation, glycogen accumulation, glucose uptake, glucose homeostasis, rapamycin resistance, kinase-independent signaling
MeSH terms: Regulatory-Associated Protein of mTOR, Rapamycin-Insensitive Companion of mTOR Protein, Age Factors, Animals, Carrier Proteins, Cells, Cultured, Energy Metabolism, Enzyme Activation, Female, Glucose, Glycogen, Mice, Inbred C57BL, Mitochondria, Muscle, Muscle Contraction, Muscular Dystrophy, Animal, Mutation, Oxidation-Reduction, Severity of Illness Index, Transduction, Genetic, Dystrophin, Phosphotransferases (Alcohol Group Acceptor), Electroporation, Mice, Knockout, Muscle, Skeletal, Sirolimus, Adaptor Proteins, Signal Transducing, Utrophin, Proto-Oncogene Proteins c-akt, Mice, Rats, TOR Serine-Threonine Kinases

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Muscle inactivation of mTOR causes metabolic and dystrophin defects leading to severe myopathy

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