Muscle inactivation of mTOR causes metabolic and dystrophin defects leading to severe myopathy
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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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Muscle-specific Rictor knockout mice do not show any overt phenotype, whereas Raptor- and mTOR-deficient mice display reduced postnatal growth due to reduced size of fast but not slow muscle fibers and a progressive muscular dystrophy phenotype.
“While muscle-specific Rictor knockout mice do not show any overt phenotype conversely, Raptor- and mTOR-deficient mice display reduced postnatal growth, due to the reduced size of fast but not slow muscle fibers and a progressive muscular dystrophy phenotype11,12.”
From Mechanisms of muscle atrophy and hypertrophy: implications in health and disease (2021) · cites this paper as [12]
Autophagy is not hyperactivated in conditional mTOR knockout and mTOR catalytically inactive mice, but instead is impaired, and this inhibition contributes to the pathological features of these animals.
“Surprisingly, autophagy is not hyperactivated in these mice, as might be expected to occur following inhibition of the mTORC1 complex (Fig. 1), but instead is impaired and this inhibition greatly contributes to the pathological features of these animals12,14.”
From Mechanisms of muscle atrophy and hypertrophy: implications in health and disease (2021) · cites this paper as [12]
Both conditional mTOR knockout and mTOR catalytically inactive transgenic mice show myofiber degeneration and a myopathic phenotype, suggesting an important pro-survival role of mTOR.
“However, both conditional mTOR knockout and mTOR catalytical inactive transgenic mice show myofiber degeneration and myopathic phenotype, suggesting an important pro-survival role of mTOR.”
From Mechanisms of muscle atrophy and hypertrophy: implications in health and disease (2021) · cites this paper as [12]
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Self-citation
- 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
- 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
- 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
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › 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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