Rapamycin blunts nutrient stimulation of eIF4G, but not PKCε phosphorylation, in skeletal muscle

TL;DR: It is shown that rapamycin treatment blocks the early (1–2 h) acute contraction‐induced increase (∼40%) in human muscle protein synthesis and dual activation of mTORC1 and ERK1/2 stimulation may be required for full stimulation of human skeletal muscleprotein synthesis.

TL;DR: Data support a fundamental role for mTORC1 activation as a key regulator of human muscle protein synthesis in response to increased EAA availability.

TL;DR: This review discusses the animal and cell culture models used and the signaling mechanisms identified in understanding regulation of protein synthesis in response to mechanical loading/resistance exercise and upstream mediators regulating mammalian target of rapamycin signaling and protein synthesis during skeletal muscle hypertrophy.

TL;DR: Understanding the physiologic and mechanistic basis of anabolic resistance could be the key to formulating new and targeted interventions that would ease the burden currently borne by the world’s aged population.

TL;DR: It is reported that mTOR forms a stoichiometric complex with raptor, an evolutionarily conserved protein with at least two roles in the mTOR pathway that through its association with mTOR regulates cell size in response to nutrient levels.

TL;DR: It is found that the rictor-mTOR complex modulates the phosphorylation of Protein Kinase C alpha (PKCalpha) and the actin cytoskeleton, suggesting that this aspect of TOR signaling is conserved between yeast and mammals.

TL;DR: Two distinct TOR complexes constitute a primordial signalling network conserved in eukaryotic evolution to control the fundamental process of cell growth.

TL;DR: Raptor is an essential scaffold for the mTOR-catalyzed phosphorylation of 4EBP1 and mediates TOR action in vivo and yields an array of phenotypes that closely resemble those produced by inactivation of Ce-TOR.