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Autophagy is essential to support skeletal muscle plasticity in response to endurance exercise
Abstract
Physical exercise is a stress that can substantially modulate cellular signaling mechanisms to promote morphological and metabolic adaptations. Skeletal muscle protein and organelle turnover is dependent on two major cellular pathways: Forkhead box class O proteins (FOXO) transcription factors that regulate two main proteolytic systems, the ubiquitin-proteasome, and the autophagy-lysosome systems, including mitochondrial autophagy, and the MTORC1 signaling associated with protein translation and autophagy inhibition. In recent years, it has been well documented that both acute and chronic endurance exercise can affect the autophagy pathway. Importantly, substantial efforts have been made to better understand discrepancies in the literature on its modulation during exercise. A single bout of endurance exercise increases autophagic flux when the duration is long enough, and this response is dependent on nutritional status, since autophagic flux markers and mRNA coding for actors involved in mitophagy are more abundant in the fasted state. In contrast, strength and resistance exercises preferentially raise ubiquitin-proteasome system activity and involve several protein synthesis factors, such as the recently characterized DAGK for mechanistic target of rapamycin activation. In this review, we discuss recent progress on the impact of acute and chronic exercise on cell component turnover systems, with particular focus on autophagy, which until now has been relatively overlooked in skeletal muscle. We especially highlight the most recent studies on the factors that can impact its modulation, including the mode of exercise and the nutritional status, and also discuss the current limitations in the literature to encourage further works on this topic.
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“Two-h AICAR + MG132 pro-autophagic cotreatment similarly induces the binding of ELAVL1/HuR protein to SQSTM1 mRNA, its loading on polysomes and its translation into de novo protein, an effect that is required to trigger autophagy and is prevented by the protein synthesis inhibitor puromycin [583].”
From Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition) 1 (2021) · cites this paper as [583]
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Metadata
- Authors
- Sanchez, A. M. J., Bernardi, H., Py, G., & Candau, R. B.
- Affiliations
- Department of Critical Care, McGill University Health Centre and Meakins-Christie Laboratories, Department of Medicine, McGill University, Montreal, Quebec, Canada;
- Institut National de la Recherche Agronomique, UMR 866 Dynamique Musculaire et Métabolisme, Montpellier, France; and
- Faculty of Sport Sciences, University of Montpellier 1, Montpellier, France
- Venue
- American Journal of Physiology-Regulatory, Integrative and Comparative Physiology
- Publisher
- American Physiological Society
- Published
- 2014-10-15
- Volume
- 307
- Issue
- 8
- Pages
- R956-R969
- ISSN
- 0363-6119
- 1522-1490
- Cited by
- 125
- References
- 46
- Language
- en
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