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

Abstract 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 a...

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Autores principales: Zhe Song, Daniel R. Moore, Nathan Hodson, Carl Ward, Jessica R. Dent, Mary F. O’Leary, Andrew M. Shaw, D. Lee Hamilton, Sovan Sarkar, Yann-Gaël Gangloff, Troy A. Hornberger, Lawrence L. Spriet, George J. Heigenhauser, Andrew Philp
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Publicado: Nature Portfolio 2017
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spelling oai:doaj.org-article:71453322f31c4042b79fba8f35f34ad72021-12-02T16:06:51ZResistance exercise initiates mechanistic target of rapamycin (mTOR) translocation and protein complex co-localisation in human skeletal muscle10.1038/s41598-017-05483-x2045-2322https://doaj.org/article/71453322f31c4042b79fba8f35f34ad72017-07-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-05483-xhttps://doaj.org/toc/2045-2322Abstract 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.Zhe SongDaniel R. MooreNathan HodsonCarl WardJessica R. DentMary F. O’LearyAndrew M. ShawD. Lee HamiltonSovan SarkarYann-Gaël GangloffTroy A. HornbergerLawrence L. SprietGeorge J. HeigenhauserAndrew PhilpNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-14 (2017)
institution DOAJ
collection DOAJ
language EN
topic Medicine
R
Science
Q
spellingShingle Medicine
R
Science
Q
Zhe Song
Daniel R. Moore
Nathan Hodson
Carl Ward
Jessica R. Dent
Mary F. O’Leary
Andrew M. Shaw
D. Lee Hamilton
Sovan Sarkar
Yann-Gaël Gangloff
Troy A. Hornberger
Lawrence L. Spriet
George J. Heigenhauser
Andrew Philp
Resistance exercise initiates mechanistic target of rapamycin (mTOR) translocation and protein complex co-localisation in human skeletal muscle
description Abstract 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.
format article
author Zhe Song
Daniel R. Moore
Nathan Hodson
Carl Ward
Jessica R. Dent
Mary F. O’Leary
Andrew M. Shaw
D. Lee Hamilton
Sovan Sarkar
Yann-Gaël Gangloff
Troy A. Hornberger
Lawrence L. Spriet
George J. Heigenhauser
Andrew Philp
author_facet Zhe Song
Daniel R. Moore
Nathan Hodson
Carl Ward
Jessica R. Dent
Mary F. O’Leary
Andrew M. Shaw
D. Lee Hamilton
Sovan Sarkar
Yann-Gaël Gangloff
Troy A. Hornberger
Lawrence L. Spriet
George J. Heigenhauser
Andrew Philp
author_sort Zhe Song
title Resistance exercise initiates mechanistic target of rapamycin (mTOR) translocation and protein complex co-localisation in human skeletal muscle
title_short Resistance exercise initiates mechanistic target of rapamycin (mTOR) translocation and protein complex co-localisation in human skeletal muscle
title_full Resistance exercise initiates mechanistic target of rapamycin (mTOR) translocation and protein complex co-localisation in human skeletal muscle
title_fullStr Resistance exercise initiates mechanistic target of rapamycin (mTOR) translocation and protein complex co-localisation in human skeletal muscle
title_full_unstemmed Resistance exercise initiates mechanistic target of rapamycin (mTOR) translocation and protein complex co-localisation in human skeletal muscle
title_sort resistance exercise initiates mechanistic target of rapamycin (mtor) translocation and protein complex co-localisation in human skeletal muscle
publisher Nature Portfolio
publishDate 2017
url https://doaj.org/article/71453322f31c4042b79fba8f35f34ad7
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