Akt/mTOR pathway is a crucial regulator of skeletal muscle hypertrophy and can prevent muscle atrophy in vivo

By S. Bodine, T. Stitt, Michael Gonzalez, W. O. Kline, Gretchen L. Stover, Roy Bauerlein, Elizabeth Zlotchenko, A. Scrimgeour, J. Lawrence, D. Glass and 1 more. Nature Cell Biology, 2001

2,782 citations recorded by the source corpus.

Subfields: Genetics, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/6f34c6d58d186aec1e743475fcf397f92a0cb4c2

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Citations in the corpus

Akt maintains cell size and survival by increasing mTOR-dependent nutrient uptake. (2002, result): “These results are also consistent with the observations that, although the maintenance of muscle mass is not dependent on the Akt, the activities of Akt and mTOR are critical for load-induced hypertrophy and recovery of mass after atrophy (Bodine et al., 2001).”
Mammalian cell size is controlled by mTOR and its downstream targets S6K1 and 4EBP1/eIF4E. (2002, background): “…PI3K-like enzymes) signals to targets other than those that are coordinately regulated by mTOR to modulate cell size; similarly, LY294002 was shown to block muscle cell hypertrophy to a greater extent than rapamycin in terminally differentiated myotubes (Bodine et al. 2001; Rommel et al. 2001).”
Bidirectional Transport of Amino Acids Regulates mTOR and Autophagy (2009, neutral): “As mTORC1 is a major regulator of cell size and tissue mass in both normal and diseased states (Bodine et al., 2001; Ohanna et al., 2005; Shaw and Cantley, 2006) it is perhaps appropriate that its activity is sensitive to both intra-cellular and circulating levels of L-glutamine.”
FOXO/4E-BP Signaling in Drosophila Muscles Regulates Organism-wide Proteostasis During Aging (2010, result): “There is an apparent contradiction between our findings and the data describing the FOXO-dependent induction of muscle atrophy inmice (Bodine et al., 2001; Sandri et al., 2004), a serious form of muscle degeneration that results in decreased muscle strength (Augustin and Partridge, 2009).”
TOR signalling in bugs, brain and brawn (2003, background): “However, muscle hypertrophy requires an increase in the rate of protein synthesis and signalling by the mTOR and the insulin-like growth factor (IGF1) pathway”
The molecular basis of skeletal muscle atrophy. (2004, background): “Muscle unloading also is associated with a decrease in both mTOR (74) and p70S6 kinase phosphorylation (10, 43), which is consistent with the decreased translation rate.”
FoxO3 controls autophagy in skeletal muscle in vivo. (2007, background): “Importantly , the rate of muscle atrophy is markedly reduced by targeted inactivation of these genes (Bodine et al., 2001a).”
mTOR Signaling in Growth, Metabolism, and Disease (2017, background): “Nonetheless, early studies of mTOR signaling in the muscle revealed that mTORC1 activation is associated with muscle hypertrophy (Bodine et al., 2001) and that both IGF-1and leucinepromote hypertrophy through the activation ofmTORC1 signaling in cultured cells and inmice (Anthony et al.”
Multiple types of skeletal muscle atrophy involve a common program of changes in gene expression (2004, background): “It stimulates the PI-3-kinase and Akt signal transduction cascade whose activation can combat denervation and disuse atrophy (58).”
Regulation of skeletal muscle growth by the IGF1-Akt/PKB pathway: insights from genetic models (2011, background): “Activation of PI3K Muscle fiber hypertrophy [69, 78 ]”
Exercise metabolism and the molecular regulation of skeletal muscle adaptation. (2013, background): “…the rate of MPS, and mediates muscle hypertrophy through protein accretion (Rennie et al., 2004). mTOR activation is critical to load-induced muscle growth, as demonstrated by the attenuation of hypertrophic responses and protein synthesis by the mTOR inhibitor, rapamycin (Bodine et al., 2001).”