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Early activation of mTORC1 signalling in response to mechanical overload is independent of phosphoinositide 3‐kinase/Akt signalling
Author(s) -
Miyazaki Mitsunori,
McCarthy John J.,
Fedele Mark J.,
Esser Karyn A.
Publication year - 2011
Publication title -
the journal of physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.802
H-Index - 240
eISSN - 1469-7793
pISSN - 0022-3751
DOI - 10.1113/jphysiol.2011.205658
Subject(s) - mtorc1 , protein kinase b , p70 s6 kinase 1 , pi3k/akt/mtor pathway , microbiology and biotechnology , phosphorylation , mapk/erk pathway , protein kinase a , chemistry , kinase , biology , signal transduction
Non‐technical summary Hypertrophy of skeletal muscle in response to resistance exercise is associated with significantly elevated rates of protein synthesis. The protein kinase mTORC1 has been shown to be a key signalling hub through which different anabolic factors (i.e. growth factors, nutrients and mechanical strain) contribute to the regulation of protein synthesis. In this study, we use an in vivo model of muscle hypertrophy to delineate the contribution of different input pathways regulating mTORC1. We found that the insulin/insulin like growth factor 1 pathway is not necessary for early activation of mTORC1 signalling but this probably occurs through activation of the ERK/TSC2 pathway. Knowledge of the key upstream pathways that modulate mTORC1 activity in vivo will provide the necessary foundation for the development of new therapeutic strategies for the maintenance of skeletal muscle mass.