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Resistance exercise initiates mechanistic target of rapamycin (mTOR) translocation and protein complex co-localisation in human skeletal muscle

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posted on 2017-07-10, 00:00 authored by Zhe Song, Daniel R Moore, Nathan Hodson, Carl Ward, Jessica R Dent, Mary F O'Leary, Andrew M Shaw, Lee HamiltonLee Hamilton, Sovan Sarkar, Yann-Gaël Gangloff, Troy A Hornberger, Lawrence L Spriet, George J Heigenhauser, Andrew Philp
The mechanistic target of rapamycin (mTOR) is a central mediator of protein synthesis in skeletal muscle. We utilized immunofluorescence approaches to study mTOR cellular distribution and protein-protein co-localisation in human skeletal muscle in the basal state as well as immediately, 1 and 3 h after an acute bout of resistance exercise in a fed (FED; 20 g Protein/40 g carbohydrate/1 g fat) or energy-free control (CON) state. mTOR and the lysosomal protein LAMP2 were highly co-localised in basal samples. Resistance exercise resulted in rapid translocation of mTOR/LAMP2 towards the cell membrane. Concurrently, resistance exercise led to the dissociation of TSC2 from Rheb and increased in the co-localisation of mTOR and Rheb post exercise in both FED and CON. In addition, mTOR co-localised with Eukaryotic translation initiation factor 3 subunit F (eIF3F) at the cell membrane post-exercise in both groups, with the response significantly greater at 1 h of recovery in the FED compared to CON. Collectively our data demonstrate that cellular trafficking of mTOR occurs in human muscle in response to an anabolic stimulus, events that appear to be primarily influenced by muscle contraction. The translocation and association of mTOR with positive regulators (i.e. Rheb and eIF3F) is consistent with an enhanced mRNA translational capacity after resistance exercise.

History

Journal

Scientific reports

Volume

7

Article number

5028

Pagination

1 - 14

Publisher

Nature Publishing Group

Location

London, Eng.

eISSN

2045-2322

Language

eng

Publication classification

C1 Refereed article in a scholarly journal

Copyright notice

2017, The Authors