Differential response of skeletal muscles to mTORC1 signaling during atrophy and hypertrophy
Open accessAbstract
BACKGROUND: Skeletal muscle mass is determined by the balance between protein synthesis and degradation. Mammalian target of rapamycin complex 1 (mTORC1) is a master regulator of protein translation and has been implicated in the control of muscle mass. Inactivation of mTORC1 by skeletal muscle-specific deletion of its obligatory component raptor results in smaller muscles and a lethal dystrophy. Moreover, raptor-deficient muscles are less oxidative through changes in the expression PGC-1α, a critical determinant of mitochondrial biogenesis. These results suggest that activation of mTORC1 might be beneficial to skeletal muscle by providing resistance to muscle atrophy and increasing oxidative function. Here, we tested this hypothesis by deletion of the mTORC1 inhibitor tuberous sclerosis complex (TSC) in muscle fibers. METHOD: Skeletal muscles of mice with an acute or a permanent deletion of raptor or TSC1 were examined using histological, biochemical and molecular biological methods. Response of the muscles to changes in mechanical load and nerve input was investigated by ablation of synergistic muscles or by denervation . RESULTS: Genetic deletion or knockdown of raptor, causing inactivation of mTORC1, was sufficient to prevent muscle growth and enhance muscle atrophy. Conversely, short-term activation of mTORC1 by knockdown of TSC induced muscle fiber hypertrophy and atrophy-resistance upon denervation, in both fast tibialis anterior (TA) and slow soleus muscles. Surprisingly, however, sustained activation of mTORC1 by genetic deletion of Tsc1 caused muscle atrophy in all but soleus muscles. In contrast, oxidative capacity was increased in all muscles examined. Consistently, TSC1-deficient soleus muscle was atrophy-resistant whereas TA underwent normal atrophy upon denervation. Moreover, upon overloading, plantaris muscle did not display enhanced hypertrophy compared to controls. Biochemical analysis indicated that the atrophy response of muscles was based on the suppressed phosphorylation of PKB/Akt via feedback inhibition by mTORC1 and subsequent increased expression of the E3 ubiquitin ligases MuRF1 and atrogin-1/MAFbx. In contrast, expression of both E3 ligases was not increased in soleus muscle suggesting the presence of compensatory mechanisms in this muscle. CONCLUSIONS: Our study shows that the mTORC1- and the PKB/Akt-FoxO pathways are tightly interconnected and differentially regulated depending on the muscle type. These results indicate that long-term activation of the mTORC1 signaling axis is not a therapeutic option to promote muscle growth because of its strong feedback induction of the E3 ubiquitin ligases involved in protein degradation.
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Cites
mTOR Signaling in Growth Control and Disease
Laplante, M., & Sabatini, D. M. (2012) · Cell · doi:10.1016/j.cell.2012.03.017 · Cited by 8,509 · see citing works
TOR signaling in growth and metabolism
Wullschleger, S., Loewith, R., & Hall, M. N. (2006) · Cell · doi:10.1016/j.cell.2006.01.016 · Cited by 5,787 · see citing works
Sandri, M., Sandri, C., Gilbert, A., Skurk, C., Calabria, E., Picard, A., Walsh, K., Schiaffino, S., Lecker, S. H., & Goldberg, A. L. (2004) · Cell · doi:10.1016/s0092-8674(04)00400-3 · Cited by 3,012 · see citing works
Bodine, S. C., Stitt, T. N., Gonzalez, M., Kline, W. O., Stover, G. L., Bauerlein, R., Zlotchenko, E., Scrimgeour, A., Lawrence, J. C., Glass, D. J., et al. (2001) · Nature Cell Biology · doi:10.1038/ncb1101-1014 · Cited by 2,752 · see citing works
Sarbassov, D. D., Ali, S. M., Kim, D.-H., Guertin, D. A., Latek, R. R., Erdjument-Bromage, H., Tempst, P., & Sabatini, D. M. (2004) · Current Biology · doi:10.1016/j.cub.2004.06.054 · Cited by 2,665 · see citing works
Transcriptional co-activator PGC-1α drives the formation of slow-twitch muscle fibres
Lin, J., Wu, H., Tarr, P. T., Zhang, C.-Y., Wu, Z., Boss, O., Michael, L. F., Puigserver, P., Isotani, E., Olson, E. N., et al. (2002) · Nature · doi:10.1038/nature00904 · Cited by 2,546 · see citing works
Mammalian TOR complex 2 controls the actin cytoskeleton and is rapamycin insensitive
Jacinto, E., Loewith, R., Schmidt, A., Lin, S., Rüegg, M. A., Hall, A., & Hall, M. N. (2004) · Nature Cell Biology · doi:10.1038/ncb1183 · Cited by 2,097 · see citing works
Puigserver, P., & Spiegelman, B. M. (2003) · Endocrine Reviews · doi:10.1210/er.2002-0012 · Cited by 2,076 · see citing works
Stitt, T. N., Drujan, D., Clarke, B. A., Panaro, F., Timofeyva, Y., Kline, W. O., Gonzalez, M., Yancopoulos, G. D., & Glass, D. J. (2004) · Molecular Cell · doi:10.1016/s1097-2765(04)00211-4 · Cited by 1,964 · see citing works
FoxO3 Controls Autophagy in Skeletal Muscle In Vivo
Mammucari, C., Milan, G., Romanello, V., Masiero, E., Rudolf, R., Del Piccolo, P., Burden, S. J., Di Lisi, R., Sandri, C., Zhao, J., et al. (2007) · Cell Metabolism · doi:10.1016/j.cmet.2007.11.001 · Cited by 1,953 · see citing works
SUnSET, a nonradioactive method to monitor protein synthesis
Schmidt, E. K., Clavarino, G., Ceppi, M., & Pierre, P. (2009) · Nature Methods · doi:10.1038/nmeth.1314 · Cited by 1,706 · see citing works
Rommel, C., Bodine, S. C., Clarke, B. A., Rossman, R., Nunez, L., Stitt, T. N., Yancopoulos, G. D., & Glass, D. J. (2001) · Nature Cell Biology · doi:10.1038/ncb1101-1009 · Cited by 1,583 · see citing works
Zhao, J., Brault, J. J., Schild, A., Cao, P., Sandri, M., Schiaffino, S., Lecker, S. H., & Goldberg, A. L. (2007) · Cell Metabolism · doi:10.1016/j.cmet.2007.11.004 · Cited by 1,489 · see citing works
mTOR controls mitochondrial oxidative function through a YY1–PGC-1α transcriptional complex
Cunningham, J. T., Rodgers, J. T., Arlow, D. H., Vazquez, F., Mootha, V. K., & Puigserver, P. (2007) · Nature · doi:10.1038/nature06322 · Cited by 1,488 · see citing works
Rapamycin-Induced Insulin Resistance Is Mediated by mTORC2 Loss and Uncoupled from Longevity
Lamming, D. W., Ye, L., Katajisto, P., Goncalves, M. D., Saitoh, M., Stevens, D. M., Davis, J. G., Salmon, A. B., Richardson, A., Ahima, R. S., et al. (2012) · Science · doi:10.1126/science.1215135 · Cited by 1,199 · see citing works
Musarò, A., McCullagh, K., Paul, A., Houghton, L., Dobrowolny, G., Molinaro, M., Barton, E. R., L Sweeney, H., & Rosenthal, N. (2001) · Nature Genetics · doi:10.1038/84839 · Cited by 1,137 · see citing works
Sandri, M., Lin, J., Handschin, C., Yang, W., Arany, Z. P., Lecker, S. H., Goldberg, A. L., & Spiegelman, B. M. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0607795103 · Cited by 974 · see citing works
Self-citationSignaling in Muscle Atrophy and Hypertrophy
Sandri, M. (2008) · Physiology · doi:10.1152/physiol.00041.2007 · Cited by 830 · see citing works
Repairing skeletal muscle: regenerative potential of skeletal muscle stem cells.
Tedesco, F. S., Dellavalle, A., Díaz-Manera, J., Messina, G., & Cossu, G. (2010) · Journal of Clinical Investigation · doi:10.1172/jci40373 · Cited by 667 · see citing works
Kwiatkowski, D. J. (2002) · Human Molecular Genetics · doi:10.1093/hmg/11.5.525 · Cited by 663 · see citing works
Bentzinger, C. F., Romanino, K., Cloëtta, D., Lin, S., Mascarenhas, J. B., Oliveri, F., Xia, J., Casanova, E., Costa, C. F., Brink, M., et al. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2008.10.002 · Cited by 640 · see citing works
Interaction between hamartin and tuberin, the TSC1 and TSC2 gene products
van Slegtenhorst, M. (1998) · Human Molecular Genetics · doi:10.1093/hmg/7.6.1053 · Cited by 565 · see citing works
Role of mTOR in podocyte function and diabetic nephropathy in humans and mice
Gödel, M., Hartleben, B., Herbach, N., Liu, S., Zschiedrich, S., Lu, S., Debreczeni-Mór, A., Lindenmeyer, M. T., Rastaldi, M.-P., Hartleben, G., et al. (2011) · Journal of Clinical Investigation · doi:10.1172/jci44774 · Cited by 547 · see citing works
mTORC1 activation in podocytes is a critical step in the development of diabetic nephropathy in mice
Inoki, K., Mori, H., Wang, J., Suzuki, T., Hong, S., Yoshida, S., Blattner, S. M., Ikenoue, T., Rüegg, M. A., Hall, M. N., et al. (2011) · Journal of Clinical Investigation · doi:10.1172/jci44771 · Cited by 538 · see citing works
The TSC1-TSC2 Complex Is Required for Proper Activation of mTOR Complex 2
Huang, J., Dibble, C. C., Matsuzaki, M., & Manning, B. D. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.00289-08 · Cited by 504 · see citing works
Adipose-Specific Knockout of raptor Results in Lean Mice with Enhanced Mitochondrial Respiration
Polak, P., Cybulski, N., Feige, J. N., Auwerx, J., Rüegg, M. A., & Hall, M. N. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2008.09.003 · Cited by 480 · see citing works
Meikle, L., Talos, D. M., Onda, H., Pollizzi, K., Rotenberg, A., Sahin, M., Jensen, F. E., & Kwiatkowski, D. J. (2007) · The Journal of Neuroscience · doi:10.1523/jneurosci.5540-06.2007 · Cited by 462 · see citing works
Conditional Activation of Akt in Adult Skeletal Muscle Induces Rapid Hypertrophy
Lai, K.-M. V., Gonzalez, M., Poueymirou, W. T., Kline, W. O., Na, E., Zlotchenko, E., Stitt, T. N., Economides, A. N., Yancopoulos, G. D., & Glass, D. J. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.21.9295-9304.2004 · Cited by 442 · see citing works
Histological parameters for the quantitative assessment of muscular dystrophy in the mdx-mouse
Briguet, A., Courdier-Fruh, I., Foster, M., Meier, T., & Magyar, J. P. (2004) · Neuromuscular Disorders · doi:10.1016/j.nmd.2004.06.008 · Cited by 417 · see citing works
Pallafacchina, G., Calabria, E., Serrano, A. L., Kalhovde, J. M., & Schiaffino, S. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.142166599 · Cited by 402 · see citing works
Fast/Glycolytic Muscle Fiber Growth Reduces Fat Mass and Improves Metabolic Parameters in Obese Mice
Izumiya, Y., Hopkins, T., Morris, C., Sato, K., Zeng, L., Viereck, J., Hamilton, J. A., Ouchi, N., LeBrasseur, N. K., & Walsh, K. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2007.11.003 · Cited by 395 · cited 2× · see citing works
“The function of active PKB/Akt to simultaneously stimulate protein synthesis and inhibit protein degradation may explain the profound hypertrophic effect of constitutively active PKB/Akt [10,11].”
Ohanna, M., Sobering, A. K., Lapointe, T., Lorenzo, L., Praud, C., Petroulakis, E., Sonenberg, N., Kelly, P. A., Sotiropoulos, A., & Pende, M. (2005) · Nature Cell Biology · doi:10.1038/ncb1231 · Cited by 392 · see citing works
Muscle inactivation of mTOR causes metabolic and dystrophin defects leading to severe myopathy
Risson, V., Mazelin, L., Roceri, M., Sanchez, H., Moncollin, V., Corneloup, C., Richard-Bulteau, H., Vignaud, A., Baas, D., Defour, A., et al. (2009) · Journal of Cell Biology · doi:10.1083/jcb.200903131 · Cited by 381 · see citing works
Arany, Z., Lebrasseur, N., Morris, C., Smith, E., Yang, W., Ma, Y., Chin, S., & Spiegelman, B. M. (2007) · Cell Metabolism · doi:10.1016/j.cmet.2006.12.003 · Cited by 370 · see citing works
β1 Integrins Regulate Myoblast Fusion and Sarcomere Assembly
Schwander, M., Leu, M., Stumm, M., Dorchies, O. M., Rüegg, U. T., Schittny, J. C., & Müller, U. (2003) · Developmental Cell · doi:10.1016/s1534-5807(03)00118-7 · Cited by 338 · see citing works
Lelliott, C. J., Medina-Gomez, G., Petrovic, N., Kis, A., Feldmann, H. M., Bjursell, M., Parker, N., Curtis, K., Campbell, M., Hu, P., et al. (2006) · PLoS Biology · doi:10.1371/journal.pbio.0040369 · Cited by 280 · cited 1× · see citing works
“Such counter-regulation between PGC1α and PGC1β has also been reported in other tissues [43].”
Calcineurin Is Required for Skeletal Muscle Hypertrophy
Dunn, S. E., Burns, J. L., & Michel, R. N. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.31.21908 · Cited by 274 · see citing works
Zechner, C., Lai, L., Zechner, J. F., Geng, T., Yan, Z., Rumsey, J. W., Collia, D., Chen, Z., Wozniak, D. F., Leone, T. C., et al. (2010) · Cell Metabolism · doi:10.1016/j.cmet.2010.11.008 · Cited by 274 · cited 1× · see citing works
“Moreover, depletion of both PGC1α and PGC1β results in much more severe loss of oxidative capacity than depletion of either protein alone [61].”
Shende, P., Plaisance, I., Morandi, C., Pellieux, C., Berthonneche, C., Zorzato, F., Krishnan, J., Lerch, R. A., Hall, M. N., Rüegg, M. A., et al. (2011) · Circulation · doi:10.1161/circulationaha.110.977066 · Cited by 239 · see citing works
Zeng, L.-H., Rensing, N. R., Zhang, B., Gutmann, D. H., Gambello, M. J., & Wong, M. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq491 · Cited by 231 · see citing works
Work-induced growth of skeletal muscle in normal and hypophysectomized rats
Goldberg, A. (1967) · American Journal of Physiology-Legacy Content · doi:10.1152/ajplegacy.1967.213.5.1193 · Cited by 218 · see citing works
Brault, J. J., Jespersen, J. G., & Goldberg, A. L. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.113092 · Cited by 217 · see citing works
Kumar, A. T., Harris, T. E., Keller, S. R., Choi, K. M., Magnuson, M. A., & Lawrence, J. C. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.01405-07 · Cited by 216 · see citing works
Critical Role for Hypothalamic mTOR Activity in Energy Balance
Mori, H., Inoki, K., Münzberg, H., Opland, D. M., Faouzi, M., Villanueva, E. C., Ikenoue, T., Kwiatkowski, D. J., MacDougald, O. A., Myers, M. G., et al. (2009) · Cell Metabolism · doi:10.1016/j.cmet.2009.03.005 · Cited by 188 · see citing works
TSC1/TSC2 and Rheb have different effects on TORC1 and TORC2 activity
Yang, Q., Inoki, K., Kim, E., & Guan, K. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0602282103 · Cited by 183 · see citing works
Rapamycin inhibits the growth and muscle-sparing effects of clenbuterol
Kline, W. O., Panaro, F. J., Yang, H., & Bodine, S. C. (2007) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00873.2006 · Cited by 177 · see citing works
Inhibition of synapse assembly in mammalian muscle in vivo by RNA interference
Kong, X. C., Barzaghi, P., & Rüegg, M. A. (2004) · EMBO Reports · doi:10.1038/sj.embor.7400065 · Cited by 131 · see citing works
Quy, P. N., Kuma, A., Pierre, P., & Mizushima, N. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.399949 · Cited by 118 · see citing works
Goodman, C. A., Miu, M. H., Frey, J. W., Mabrey, D. M., Lincoln, H. C., Ge, Y., Chen, J., & Hornberger, T. A. (2010) · Molecular Biology of the Cell · doi:10.1091/mbc.e10-05-0454 · Cited by 116 · see citing works
Biochemical properties of overloaded fast-twitch skeletal muscle
Baldwin, K. M., Valdez, V., Herrick, R. E., MacIntosh, A. M., & Roy, R. R. (1982) · Journal of Applied Physiology · doi:10.1152/jappl.1982.52.2.467 · Cited by 110 · see citing works
Molecular Mechanisms and Treatment Options for Muscle Wasting Diseases
Rüegg, M. A., & Glass, D. J. (2011) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-010510-100537 · Cited by 109 · see citing works
Critical roles for the TSC-mTOR pathway in β-cell function
Mori, H., Inoki, K., Opland, D. M., Münzberg, H., Villanueva, E. C., Faouzi, M., Ikenoue, T., Kwiatkowski, D. J., MacDougald, O. A., Myers, M. G., et al. (2009) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00262.2009 · Cited by 103 · see citing works
Dunn, S. E., & Michel, R. N. (1997) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.1997.273.2.c371 · Cited by 60 · see citing works
Physiological characteristics of re‐innervation of skeletal muscle in the mouse
Tonge, D. (1974) · The Journal of Physiology · doi:10.1113/jphysiol.1974.sp010645 · Cited by 54 · see citing works
Insulin-like growth factor I slows the rate of denervation induced skeletal muscle atrophy
Shavlakadze, T., White, J. D., Davies, M. J., Hoh, J. F. Y., & Grounds, M. D. (2005) · Neuromuscular Disorders · doi:10.1016/j.nmd.2004.10.013 · Cited by 51 · see citing works
Calpain 3 mRNA expression in mice after denervation and during muscle regeneration
Stockholm, D., Hérasse, M., Marchand, S., Praud, C., Roudaut, C., Richard, I., Sébille, A., & Beckmann, J. S. (2001) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.2001.280.6.c1561 · Cited by 49 · see citing works
Romanino, K., Mazelin, L., Albert, V., Conjard‐Duplany, A., Lin, S., Bentzinger, C. F., Handschin, C., Puigserver, P., Zorzato, F., Schaeffer, L., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1111448109 · Cited by 44 · see citing works
Dunant, P., Larochelle, N., Thirion, C., Stucka, R., Ursu, D., Petrof, B. J., Wolf, E., & Lochmüller, H. (2003) · Molecular Therapy · doi:10.1016/s1525-0016(03)00129-1 · Cited by 44 · see citing works
Muscle atrophy in transgenic mice expressing a human TSC1 transgene
Wan, M., Wu, X., Guan, K., Han, M., Zhuang, Y., & Xu, T. (2006) · FEBS Letters · doi:10.1016/j.febslet.2006.09.008 · Cited by 35 · see citing works
Expression pattern of myostatin in gastrocnemius muscle of rats after sciatic nerve crush injury
Liu, M., Zhang, D., Shao, C., Liu, J., Ding, F., & Gu, X. (2007) · Muscle & Nerve · doi:10.1002/mus.20749 · Cited by 30 · see citing works
Tamaki, T., Uchiyama, Y., Okada, Y., Tono, K., Nitta, M., Hoshi, A., & Akatsuka, A. (2009) · Histochemistry and Cell Biology · doi:10.1007/s00418-009-0585-1 · Cited by 13 · see citing works
Flagged first, then by citations
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Satellite Cells and Skeletal Muscle Regeneration
Dumont, N. A., Bentzinger, C. F., Sincennes, M., & Rudnicki, M. A. (2015) · Comprehensive Physiology · doi:10.1002/cphy.c140068 · Cited by 719 · see citing works
Protein breakdown in muscle wasting: Role of autophagy-lysosome and ubiquitin-proteasome
Sandri, M. (2013) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2013.04.023 · Cited by 689 · see citing works
Signaling pathways controlling skeletal muscle mass
Egerman, M. A., & Glass, D. J. (2014) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238.2013.857291 · Cited by 555 · see citing works
Mechanisms Regulating Neuromuscular Junction Development and Function and Causes of Muscle Wasting
Tintignac, L. A. J., Brenner, H.-R., & Rüegg, M. A. (2015) · Physiological Reviews · doi:10.1152/physrev.00033.2014 · Cited by 422 · see citing works
Leal, L. G., Lopes, M. A., & Batista, M. L. (2018) · Frontiers in Physiology · doi:10.3389/fphys.2018.01307 · Cited by 382 · see citing works
“Skeletal Muscle as an Immunogenic Organ The Concept of Myokines The SkM is a highly organized tissue at the micro and macroscopic level and is the body’s main protein reserve (Hornberger, 2011; Bentzinger et al., 2013).”
BackgroundThe mTOR–Autophagy Axis and the Control of Metabolism
Deleyto-Seldas, N., & Efeyan, A. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.655731 · Cited by 360 · see citing works
Castets, P., Lin, S., Rion, N., Di Fulvio, S., Romanino, K., Guridi, M., Frank, S., Tintignac, L. A., Sinnreich, M., & Rüegg, M. A. (2013) · Cell Metabolism · doi:10.1016/j.cmet.2013.03.015 · Cited by 302 · see citing works
mTOR signaling in cellular and organismal energetics
Albert, V., & Hall, M. N. (2015) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2014.12.001 · Cited by 304 · see citing works
Multiple amino acid sensing inputs to mTORC1
Shimobayashi, M., & Hall, M. (2015) · Cell Research · doi:10.1038/cr.2015.146 · Cited by 216 · see citing works
The molecular athlete: exercise physiology from mechanisms to medals
Furrer, R., Hawley, J. A., & Handschin, C. (2023) · Physiological Reviews · doi:10.1152/physrev.00017.2022 · Cited by 232 · see citing works
Roberts, M. D., McCarthy, J. J., Hornberger, T. A., Phillips, S. M., Mackey, A. L., Nader, G. A., Boppart, M. D., Kavazis, A. N., Reidy, P. T., Ogasawara, R., et al. (2023) · Physiological Reviews · doi:10.1152/physrev.00039.2022 · Cited by 214 · see citing works
Signaling Pathways That Control Muscle Mass
Vainshtein, A., & Sandri, M. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21134759 · Cited by 214 · see citing works
Ribosome biogenesis: Emerging evidence for a central role in the regulation of skeletal muscle mass
Chaillou, T., Kirby, T. J., & McCarthy, J. J. (2014) · Journal of Cellular Physiology · doi:10.1002/jcp.24604 · Cited by 211 · see citing works
Tang, H., Inoki, K., Brooks, S. V., Okazawa, H., Lee, M. C., Wang, J., Kim, M., Kennedy, C. L., Macpherson, P. C. D., Ji, X., et al. (2019) · Aging Cell · doi:10.1111/acel.12943 · Cited by 191 · see citing works
Balanced mTORC1 Activity in Oligodendrocytes Is Required for Accurate CNS Myelination
Lebrun-Julien, F., Bachmann, L., Norrmén, C., Trötzmüller, M., Köfeler, H., Rüegg, M., Hall, M., & Suter, U. (2014) · Journal of Neuroscience · doi:10.1523/jneurosci.1105-14.2014 · Cited by 174 · see citing works
Nunes, E. A., Stokes, T., McKendry, J., Currier, B. S., & Phillips, S. M. (2022) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00425.2021 · Cited by 183 · see citing works
Wnt7a stimulates myogenic stem cell motility and engraftment resulting in improved muscle strength
Bentzinger, C. F., von Maltzahn, J., Dumont, N. A., Stark, D. A., Wang, Y. X., Nhan, K., Frenette, J., Cornelison, D., & Rudnicki, M. A. (2014) · The Journal of Cell Biology · doi:10.1083/jcb.201310035 · Cited by 163 · see citing works
You, J.-S., Mcnally, R. M., Jacobs, B. L., Privett, R. E., Gundermann, D. M., Lin, K.-H., Steinert, N. D., Goodman, C. A., & Hornberger, T. A. (2019) · The FASEB Journal · doi:10.1096/fj.201801653rr · Cited by 149 · see citing works
Tang, H., Inoki, K., Lee, M. C., Wright, E., Khuong, A., Khuong, A., Sugiarto, S., Garner, M. S., Paik, J., DePinho, R. A., et al. (2014) · Science Signaling · doi:10.1126/scisignal.2004809 · Cited by 142 · see citing works
Satellite Cells and Skeletal Muscle Regeneration
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Dyle, M. C., Ebert, S. M., Cook, D. P., Kunkel, S. D., Fox, D. K., Bongers, K. S., Bullard, S. A., Dierdorff, J. M., & Adams, C. M. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.556241 · Cited by 138 · see citing works
Goodman, C. A. (2013) · Reviews of physiology, biochemistry and pharmacology · doi:10.1007/112_2013_17 · Cited by 139 · see citing works
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Forkhead Box O Signaling Pathway in Skeletal Muscle Atrophy
Chen, K., Gao, P., Li, Z., Dai, A., Yang, M. W. O., Chen, S., Su, J., Deng, Z., & Li, L. (2022) · American Journal Of Pathology · doi:10.1016/j.ajpath.2022.09.003 · Cited by 122 · see citing works
Muscle-specific 4E-BP1 signaling activation improves metabolic parameters during aging and obesity
Tsai, S., Sitzmann, J. M., Dastidar, S. G., Rodriguez, A. A., Vu, S. L., McDonald, C. E., Academia, E. C., O’Leary, M. N., Ashe, T. D., Spada, A. R. L., et al. (2015) · Journal of Clinical Investigation · doi:10.1172/jci77361 · Cited by 130 · see citing works
White, Z. R., Terrill, J. R., White, R. B., McMahon, C., Sheard, P., Grounds, M. D., & Shavlakadze, T. (2016) · Skeletal Muscle · doi:10.1186/s13395-016-0117-3 · Cited by 119 · see citing works
Liver alanine catabolism promotes skeletal muscle atrophy and hyperglycaemia in type 2 diabetes
Okun, J. G., Rusu, P. M., Chan, A. Y., Wu, Y., Yap, Y. W., Sharkie, T., Schumacher, J., Schmidt, K. V., Roberts‐Thomson, K. M., Russell, R., et al. (2021) · Nature Metabolism · doi:10.1038/s42255-021-00369-9 · Cited by 116 · see citing works
Cellular and molecular mechanisms of sarcopenia: The S100B perspective
Riuzzi, F., Sorci, G., Arcuri, C., Giambanco, I., Bellezza, I., Minelli, A., & Donato, R. (2018) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.12363 · Cited by 114 · see citing works
mTORC1 and PKB/Akt control the muscle response to denervation by regulating autophagy and HDAC4
Castets, P., Rion, N., Théodore, M., Falcetta, D., Lin, S., Reischl, M., Wild, F., Guérard, L., Eickhorst, C., Brockhoff, M., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-11227-4 · Cited by 112 · see citing works
Understanding the Role of Exercise in Cancer Cachexia Therapy
Hardee, J. P., Counts, B. R., & Carson, J. A. (2017) · American Journal of Lifestyle Medicine · doi:10.1177/1559827617725283 · Cited by 108 · see citing works
Pompe Disease: New Developments in an Old Lysosomal Storage Disorder
Meena, N. K., & Raben, N. (2020) · Biomolecules · doi:10.3390/biom10091339 · Cited by 112 · see citing works
Activation of mTORC1 in skeletal muscle regulates whole-body metabolism through FGF21
Guridi, M., Tintignac, L. A. J., Lin, S., Kupr, B., Castets, P., & Rüegg, M. A. (2015) · Science Signaling · doi:10.1126/scisignal.aab3715 · Cited by 99 · see citing works
Chaturvedi, V., Dye, D. E., Kinnear, B. F., Kuppevelt, T. H. V., Grounds, M. D., & Coombe, D. R. (2015) · PLoS ONE · doi:10.1371/journal.pone.0127675 · Cited by 95 · see citing works
Crossland, H., Kazi, A. A., Lang, C. H., Timmons, J. A., Pierre, P., Wilkinson, D. J., Smith, K., Szewczyk, N. J., & Atherton, P. J. (2013) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00541.2012 · Cited by 95 · see citing works
Modulation of mTOR signaling as a strategy for the treatment of Pompe disease
Lim, J., Li, L., Shirihai, O. S., Trudeau, K. M., Puertollano, R., & Raben, N. (2017) · EMBO Molecular Medicine · doi:10.15252/emmm.201606547 · Cited by 94 · see citing works
Targeting deregulated AMPK/mTORC1 pathways improves muscle function in myotonic dystrophy type I
Brockhoff, M., Rion, N., Chojnowska, K., Wiktorowicz, T., Eickhorst, C., Erne, B., Frank, S., Angelini, C. I., Furling, D., Rüegg, M. A., et al. (2017) · Journal of Clinical Investigation · doi:10.1172/jci89616 · Cited by 87 · see citing works
Börsch, A., Ham, D. J., Mittal, N., Tintignac, L. A., Migliavacca, E., Feige, J. N., Rüegg, M. A., & Zavolan, M. (2021) · Communications Biology · doi:10.1038/s42003-021-01723-z · Cited by 85 · see citing works
Jaiswal, N., Gavin, M., Loro, E., Sostre‐Colón, J., Roberson, P. A., Uehara, K., Rivera‐Fuentes, N., Neinast, M., Arany, Z., Kimball, S. R., et al. (2022) · Journal of Cachexia, Sarcopenia and Muscle · doi:10.1002/jcsm.12846 · Cited by 79 · see citing works
Dkk3 dependent transcriptional regulation controls age related skeletal muscle atrophy
Yin, J., Yang, L., Xie, Y., Liu, Y., Li, S., Yang, W., Xu, B., Ji, H., Ding, L., Wang, K., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-04038-6 · Cited by 72 · see citing works
Skeletal muscle mTORC1 regulates neuromuscular junction stability
Baraldo, M., Geremia, A., Pirazzini, M., Nogara, L., Solagna, F., Türk, C., Nolte, H., Romanello, V., Megighian, A., Boncompagni, S., et al. (2020) · Journal of Cachexia, Sarcopenia and Muscle · doi:10.1002/jcsm.12496 · Cited by 76 · see citing works
Ferretti, R., Moura, E. G., dos Santos, V. C., Caldeira, E. J., Conte, M., Matsumura, C. Y., Pertille, A., & Mosqueira, M. (2018) · PLoS ONE · doi:10.1371/journal.pone.0199728 · Cited by 72 · see citing works
Aoyama, S., Kim, H., Hirooka, R., Tanaka, M., Shimoda, T., Chijiki, H., Kojima, S., Sasaki, K., Takahashi, K., Makino, S., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2021.109336 · Cited by 73 · see citing works
Gehlert, S., Suhr, F., Gutsche, K., Willkomm, L., Kern, J., Jacko, D., Knicker, A. J., Schiffer, T., Wackerhage, H., & Bloch, W. (2014) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-014-1579-y · Cited by 71 · see citing works
Redox regulation of autophagy in skeletal muscle
Rodney, G. G., Pal, R., & Abo‐Zahrah, R. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.05.010 · Cited by 72 · see citing works
Circadian clock regulation of skeletal muscle growth and repair
Chatterjee, S., & Ma, K. (2016) · F1000Research · doi:10.12688/f1000research.9076.1 · Cited by 66 · see citing works
Damanti, S., Azzolino, D., Roncaglione, C., Arosio, B., Rossi, P., & Cesari, M. (2019) · Nutrients · doi:10.3390/nu11091991 · Cited by 62 · see citing works
Paez, H. G., Pitzer, C. R., & Alway, S. E. (2023) · Cells · doi:10.3390/cells12020249 · Cited by 65 · see citing works
A role for Raptor phosphorylation in the mechanical activation of mTOR signaling
Frey, J. W., Jacobs, B. L., Goodman, C. A., & Hornberger, T. A. (2013) · Cellular Signalling · doi:10.1016/j.cellsig.2013.11.009 · Cited by 60 · see citing works
Irisin and Autophagy: First Update
Pesce, M., Ballerini, P., Paolucci, T., Puca, I., Farzaei, M. H., & Patruno, A. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21207587 · Cited by 59 · see citing works
Biology of Activating Transcription Factor 4 (ATF4) and Its Role in Skeletal Muscle Atrophy
Ebert, S. M., Rasmussen, B. B., Judge, A. R., Judge, S. M., Larsson, L., Wek, R. C., Anthony, T. G., Marcotte, G. R., Miller, M. J., Yorek, M. A., et al. (2021) · Journal of Nutrition · doi:10.1093/jn/nxab440 · Cited by 61 · see citing works
Bilski, J., Mazur-Biały, A. I., Wierdak, M., & Brzozowski, T. (2013) · PubMed · Cited by 55 · see citing works
Resistance Exercise-Induced Hypertrophy: A Potential Role for Rapamycin-Insensitive mTOR
Ogasawara, R., Jensen, T. E., Goodman, C. A., & Hornberger, T. A. (2019) · Exercise and Sport Sciences Reviews · doi:10.1249/jes.0000000000000189 · Cited by 58 · see citing works
Dutchak, P. A., Estill-Terpack, S. J., Plec, A. A., Zhao, X., Yang, C., Chen, J., Ko, B., Deberardinis, R. J., Yu, Y., & Tu, B. P. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.04.058 · Cited by 53 · see citing works
Cai, X., Zhu, C., Xu, Y., Jing, Y., Yuan, Y., Wang, L., Wang, S., Zhu, X., Gao, P., Zhang, Y., et al. (2016) · Scientific Reports · doi:10.1038/srep26802 · Cited by 54 · see citing works
RetractedWeight Pulling: A Novel Mouse Model of Human Progressive Resistance Exercise
Zhu, W. G., Hibbert, J. E., Lin, K., Steinert, N. D., Lemens, J. L., Jorgenson, K. W., Newman, S. M., Lamming, D. W., & Hornberger, T. A. (2021) · Cells · doi:10.3390/cells10092459 · Cited by 54 · see citing works
Muscle aging and sarcopenia: The pathology, etiology, and most promising therapeutic targets
Grima-Terrén, M., Campanario, S., Ramírez‐Pardo, I., Cisneros, A., Hong, X., Perdiguero, E., Serrano, A. L., Isern, J., & Muñoz‐Cánoves, P. (2024) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2024.101319 · Cited by 49 · see citing works
Pérez‐Schindler, J., Summermatter, S., Santos, G., Zorzato, F., & Handschin, C. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1312039110 · Cited by 46 · see citing works
Dual roles of mTORC1-dependent activation of the ubiquitin-proteasome system in muscle proteostasis
Kaiser, M. S., Milan, G., Ham, D. J., Lin, S., Oliveri, F., Chojnowska, K., Tintignac, L. A. J., Mittal, N., Zimmerli, C. E., Glass, D. J., et al. (2022) · Communications Biology · doi:10.1038/s42003-022-04097-y · Cited by 46 · see citing works
Nicks, J., Lee, S., Harris, A. B., Falk, D. J., Todd, A. G., Arredondo, K., Dunn, W. A., & Notterpek, L. M. (2014) · Neurobiology of Disease · doi:10.1016/j.nbd.2014.06.023 · Cited by 41 · see citing works
Zoledronic Acid Improves Muscle Function in Healthy Mice Treated with Chemotherapy
Hain, B. A., Jude, B., Xu, H.-F., Smuin, D., Fox, E. J., Elfar, J. C., & Waning, D. L. (2020) · Journal of Bone and Mineral Research · doi:10.1002/jbmr.3890 · Cited by 34 · see citing works
Alterations to mTORC1 signaling in the skeletal muscle differentially affect whole-body metabolism
Guridi, M., Kupr, B., Romanino, K., Lin, S., Falcetta, D., Tintignac, L. A. J., & Rüegg, M. A. (2016) · Skeletal Muscle · doi:10.1186/s13395-016-0084-8 · Cited by 39 · see citing works
Systematic review of the synergist muscle ablation model for compensatory hypertrophy
Terena, S. M. L., Fernandes, K. P. S., Bussadori, S. K., Deana, A. M., & Mesquita‐Ferrari, R. A. (2017) · Revista da Associação Médica Brasileira · doi:10.1590/1806-9282.63.02.164 · Cited by 38 · see citing works
Knockdown of the E3 ubiquitin ligase UBR5 and its role in skeletal muscle anabolism
Turner, D. C., Hughes, D. C., Baehr, L. M., Seaborne, R. A. E., Viggars, M. R., Jarvis, J. C., Gorski, P. P., Stewart, C. E., Owens, D. J., Bodine, S. C., et al. (2020) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00432.2020 · Cited by 38 · see citing works
Tumor promoter-induced cellular senescence: cell cycle arrest followed by geroconversion
Leontieva, O. V., & Blagosklonny, M. V. (2014) · Oncotarget · doi:10.18632/oncotarget.3011 · Cited by 36 · see citing works
Solsona, R., Pavlin, L., Bernardi, H., & Sanchez, A. M. J. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22052741 · Cited by 39 · see citing works
Ham, A. S., Chojnowska, K., Tintignac, L. A. J., Lin, S., Schmidt, A., Ham, D. J., Sinnreich, M., & Rüegg, M. A. (2019) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.12505 · Cited by 36 · see citing works
Molecular Mechanisms Underlying Muscle Wasting in Huntington’s Disease
Bozzi, M., & Sciandra, F. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21218314 · Cited by 36 · see citing works
Jacobs, B. L., McNally, R. M., Kim, K., Blanco, R., Privett, R. E., You, J., & Hornberger, T. A. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.777805 · Cited by 34 · see citing works
mTORC1 in energy expenditure: consequences for obesity
Allard, C., Miralpeix, C., López-Gambero, A. J., & Cota, D. (2024) · Nature Reviews Endocrinology · doi:10.1038/s41574-023-00934-0 · Cited by 29 · see citing works
Molecular mechanisms and treatment targets of muscle wasting and cachexia in heart failure
Ebner, N., Elsner, S., Springer, J., & von Haehling, S. (2014) · Current Opinion in Supportive and Palliative Care · doi:10.1097/spc.0000000000000030 · Cited by 33 · see citing works
Contraction‐regulated mTORC1 and protein synthesis: Influence of AMPK and glycogen
Knudsen, J. R., Li, Z., Persson, K. W., Li, J., Henríquez‐Olguín, C., & Jensen, T. E. (2020) · The Journal of Physiology · doi:10.1113/jp279780 · Cited by 33 · see citing works
Recent advances in mitochondrial turnover during chronic muscle disuse
Tryon, L. D., Vainshtein, A., Memme, J. M., Crilly, M. J., & Hood, D. A. (2014) · Integrative Medicine Research · doi:10.1016/j.imr.2014.09.001 · Cited by 33 · see citing works
Zhang, Q., Duplany, A., Moncollin, V., Mouradian, S., Goillot, E., Mazelin, L., Gauthier, K., Streichenberger, N., Angleraux, C., Chen, J., et al. (2019) · Journal of Cachexia, Sarcopenia and Muscle · doi:10.1002/jcsm.12336 · Cited by 31 · see citing works
Crombie, E. M., Kim, S., Adamson, S. S., Dong, H., Lu, T., Wu, Y., Wu, Y., Levy, Y., Stimple, N., Lam, W. M. R., et al. (2022) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.13121 · Cited by 30 · see citing works
Graber, T. G., Fry, C., Brightwell, C. R., Moro, T., Maroto, R., Bhattarai, N., Porter, C., Wakamiya, M., & Rasmussen, B. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.005970 · Cited by 27 · see citing works
Sato, Y., Sato, Y., Obeng, K. A., & Yoshizawa, F. (2018) · Nutrition Research · doi:10.1016/j.nutres.2018.05.006 · Cited by 29 · see citing works
Salucci, S., Bartoletti‐Stella, A., Bavelloni, A., Aramini, B., Blalock, W. L., Fabbri, F., Vannini, I., Sambri, V., Stella, F., & Faenza, I. (2022) · Nutrients · doi:10.3390/nu14173567 · Cited by 30 · see citing works
Ginseng and ginsenosides: Therapeutic potential for sarcopenia
Zha, W., Sun, Y., Gong, W., Li, L., Kim, W., & Li, H. (2022) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2022.113876 · Cited by 29 · see citing works
4E‐BP1 and 4E‐BP2 double knockout mice are protected from aging‐associated sarcopenia
Bacquer, O. L., Combe, K., Patrac, V., Ingram, B., Combaret, L., Dardevet, D., Montaurier, C., Salles, J., Giraudet, C., Guillet, C., et al. (2019) · Journal of Cachexia, Sarcopenia and Muscle · doi:10.1002/jcsm.12412 · Cited by 25 · see citing works
Cicatiello, A. G., Sagliocchi, S., Nappi, A., Cicco, E. D., Miro, C., Murolo, M., Stornaiuolo, M., & Dentice, M. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.110409 · Cited by 28 · see citing works
Zhao, Y.-C., & Gao, B. (2024) · European Journal of Applied Physiology · doi:10.1007/s00421-024-05549-5 · Cited by 31 · see citing works
You, J., Kim, K., Steinert, N. D., Chen, J., & Hornberger, T. A. (2021) · Cell Death Discovery · doi:10.1038/s41420-021-00460-w · Cited by 27 · see citing works
Ligands for FKBP12 Increase Ca2+ Influx and Protein Synthesis to Improve Skeletal Muscle Function
Lee, C. S., Georgiou, D. K., Dagnino-Acosta, A., Xu, J., Ismailov, I. I., Knoblauch, M. A., Monroe, T. O., Ji, R., Hanna, A. D., Joshi, A., et al. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.586289 · Cited by 26 · see citing works
Ferry, A., Schuh, M., Parlakian, A., Mgrditchian, T., Valnaud, N., Joanne, P., Butler-Browne, G. S., Agbulut, O., & METZGER, D. (2014) · Endocrinology · doi:10.1210/en.2014-1195 · Cited by 25 · see citing works
PGC-1α in osteoarthritic chondrocytes: From mechanism to target of action
Wang, H., Su, J., Yu, M., Xia, Y., & Wei, Y. (2023) · Frontiers in Pharmacology · doi:10.3389/fphar.2023.1169019 · Cited by 24 · see citing works
A muscle-specific UBE2O/AMPKα2 axis promotes insulin resistance and metabolic syndrome in obesity
Vila, I. K., Park, M. K., Setijono, S. R., Yao, Y., Kim, H., Badin, P.-M., Choi, S., Narkar, V. A., Choi, S., Chung, J., et al. (2019) · JCI Insight · doi:10.1172/jci.insight.128269 · Cited by 23 · see citing works
Aging, Skeletal Muscle, and Epigenetics
Stewart, C. E., & Sharples, A. P. (2021) · Plastic & Reconstructive Surgery · doi:10.1097/prs.0000000000009670 · Cited by 22 · see citing works
Huang, J., Luo, X., Zeng, L., Huang, Z., Huang, M., You, W., & Ke, C. (2018) · Scientific Reports · doi:10.1038/s41598-018-35202-z · Cited by 21 · see citing works
Ballinger, T. J., Thompson, W. R., & Guise, T. A. (2022) · Breast Cancer Research · doi:10.1186/s13058-022-01576-2 · Cited by 22 · see citing works
Resistance Training Improves Hypertrophic and Mitochondrial Adaptation in Skeletal Muscle
Zhao, Y., & Wu, Y. (2023) · International Journal of Sports Medicine · doi:10.1055/a-2059-9175 · Cited by 20 · see citing works
CL316,243, a β3-adrenergic receptor agonist, induces muscle hypertrophy and increased strength
Puzzo, D., Raiteri, R., Castaldo, C., Capasso, R., Pagano, E., Tedesco, M., Gulisano, W., Drozd, L., Lippiello, P., Palmeri, A., et al. (2016) · Scientific Reports · doi:10.1038/srep37504 · Cited by 19 · see citing works
Maruyama, Y., Ikeda, C., Wakabayashi, K., Ato, S., & Ogasawara, R. (2020) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00578.2019 · Cited by 18 · see citing works
Bacquer, O. L., Combe, K., Montaurier, C., Salles, J., Giraudet, C., Patrac, V., Domingues-Faria, C., Guillet, C., Louche, K., Boirie, Y., et al. (2017) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.201700128 · Cited by 16 · see citing works
Obesity Augments Glucocorticoid-Dependent Muscle Atrophy in Male C57BL/6J Mice
Gunder, L. C., Harvey, I. C., Redd, J. R., Davis, C. S., AL-Tamimi, A., Brooks, S. V., & Bridges, D. (2020) · Biomedicines · doi:10.3390/biomedicines8100420 · Cited by 15 · see citing works
Sato, Y., Sato, Y., Suzuki, R., Obeng, K. A., & Yoshizawa, F. (2018) · Experimental Cell Research · doi:10.1016/j.yexcr.2018.02.002 · Cited by 14 · see citing works
Self‐transducible LRS‐UNE‐L peptide enhances muscle regeneration
Baek, M., Cho, H., Min, D. S., Choi, C. S., & Yoon, M. (2022) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.12947 · Cited by 13 · see citing works
Rindom, E., Herskind, J., Blaauw, B., Overgaard, K., Vissing, K., & de Paoli, F. V. (2020) · Acta Physiologica · doi:10.1111/apha.13540 · Cited by 13 · see citing works
Fallone, L., Walzer, T., & Marçais, A. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241612736 · Cited by 11 · see citing works
Gehlert, S., Klinz, F., Willkomm, L., Schiffer, T., Suhr, F., & Bloch, W. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms17050646 · Cited by 12 · see citing works
Ham, D. J., Semeraro, M., Berger, B. M., McGowan, T. J., Lin, S., Maino, E., Oliveri, F., & Rüegg, M. A. (2025) · Nature Communications · doi:10.1038/s41467-025-58542-7 · Cited by 10 · see citing works
- Authors
- Bentzinger, C. F., Lin, S., Romanino, K., Castets, P., Guridi, M., Summermatter, S., Handschin, C., Tintignac, L. A., Hall, M. N., & Rüegg, M. A.
- Affiliations
- University of Basel (CH)
- Corresponding author
- Rüegg, Markus A
- ORCID
- Venue
- Skeletal Muscle
- Published
- 2013-03-06
- Volume
- 3
- Issue
- 1
- Pages
- 6-6
- ISSN
- 2044-5040 (ISSN-L)
- PMC
- PMC3622636
- OpenAlex
- W2149451793
- Cited by
- 153
- References
- 61
- Citations by year
- 2026: 4 · 2025: 13 · 2024: 14 · 2023: 8 · 2022: 10 · 2021: 14 · 2020: 11 · 2019: 16 · 2018: 11 · 2017: 8 · 2016: 11 · 2015: 10 · 2014: 14 · 2013: 8
- FWCI
- 6.42
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- cc-by
- Locations
- Skeletal Muscle (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- edoc (University of Basel) (acceptedVersion)
- Archive ouverte UNIGE (University of Geneva) (submittedVersion, cc-by)
- HAL (submittedVersion, cc-by)
- edoc (University of Basel)
- Funders
- National Science Foundation
- Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Muscle metabolism and nutrition
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › PI3K/AKT/mTOR signaling in cancer
- Keywords
- mTORC1 signaling, skeletal muscle atrophy, muscle hypertrophy, raptors, tuberous sclerosis complex 1, denervation, muscle overload, oxidative capacity, PGC-1α, mitochondrial biogenesis, Akt signaling, FOXO, MuRF1, atrogin-1/MAFbx, E3 ubiquitin ligase, muscle fiber type, soleus muscle
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