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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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) |
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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 |
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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 |
work_keys_str_mv |
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