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mTOR as a Key Regulator in Maintaining Skeletal Muscle Mass

Maintenance of skeletal muscle mass is regulated by the balance between anabolic and catabolic processes. Mammalian target of rapamycin (mTOR) is an evolutionarily conserved serine/threonine kinase, and is known to play vital roles in protein synthesis. Recent findings have continued to refine our u...

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Autor principal: Yoon, Mee-Sup
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5650960/
https://www.ncbi.nlm.nih.gov/pubmed/29089899
http://dx.doi.org/10.3389/fphys.2017.00788
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author Yoon, Mee-Sup
author_facet Yoon, Mee-Sup
author_sort Yoon, Mee-Sup
collection PubMed
description Maintenance of skeletal muscle mass is regulated by the balance between anabolic and catabolic processes. Mammalian target of rapamycin (mTOR) is an evolutionarily conserved serine/threonine kinase, and is known to play vital roles in protein synthesis. Recent findings have continued to refine our understanding of the function of mTOR in maintaining skeletal muscle mass. mTOR controls the anabolic and catabolic signaling of skeletal muscle mass, resulting in the modulation of muscle hypertrophy and muscle wastage. This review will highlight the fundamental role of mTOR in skeletal muscle growth by summarizing the phenotype of skeletal-specific mTOR deficiency. In addition, the evidence that mTOR is a dual regulator of anabolism and catabolism in skeletal muscle mass will be discussed. A full understanding of mTOR signaling in the maintenance of skeletal muscle mass could help to develop mTOR-targeted therapeutics to prevent muscle wasting.
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spelling pubmed-56509602017-10-31 mTOR as a Key Regulator in Maintaining Skeletal Muscle Mass Yoon, Mee-Sup Front Physiol Physiology Maintenance of skeletal muscle mass is regulated by the balance between anabolic and catabolic processes. Mammalian target of rapamycin (mTOR) is an evolutionarily conserved serine/threonine kinase, and is known to play vital roles in protein synthesis. Recent findings have continued to refine our understanding of the function of mTOR in maintaining skeletal muscle mass. mTOR controls the anabolic and catabolic signaling of skeletal muscle mass, resulting in the modulation of muscle hypertrophy and muscle wastage. This review will highlight the fundamental role of mTOR in skeletal muscle growth by summarizing the phenotype of skeletal-specific mTOR deficiency. In addition, the evidence that mTOR is a dual regulator of anabolism and catabolism in skeletal muscle mass will be discussed. A full understanding of mTOR signaling in the maintenance of skeletal muscle mass could help to develop mTOR-targeted therapeutics to prevent muscle wasting. Frontiers Media S.A. 2017-10-17 /pmc/articles/PMC5650960/ /pubmed/29089899 http://dx.doi.org/10.3389/fphys.2017.00788 Text en Copyright © 2017 Yoon. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Physiology
Yoon, Mee-Sup
mTOR as a Key Regulator in Maintaining Skeletal Muscle Mass
title mTOR as a Key Regulator in Maintaining Skeletal Muscle Mass
title_full mTOR as a Key Regulator in Maintaining Skeletal Muscle Mass
title_fullStr mTOR as a Key Regulator in Maintaining Skeletal Muscle Mass
title_full_unstemmed mTOR as a Key Regulator in Maintaining Skeletal Muscle Mass
title_short mTOR as a Key Regulator in Maintaining Skeletal Muscle Mass
title_sort mtor as a key regulator in maintaining skeletal muscle mass
topic Physiology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5650960/
https://www.ncbi.nlm.nih.gov/pubmed/29089899
http://dx.doi.org/10.3389/fphys.2017.00788
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