FoxO3 Controls Autophagy in Skeletal Muscle In Vivo
Open accessAbstract
Autophagy allows cell survival during starvation through the bulk degradation of proteins and organelles by lysosomal enzymes. However, the mechanisms responsible for the induction and regulation of the autophagy program are poorly understood. Here we show that the FoxO3 transcription factor, which plays a critical role in muscle atrophy, is necessary and sufficient for the induction of autophagy in skeletal muscle in vivo. Akt/PKB activation blocks FoxO3 activation and autophagy, and this effect is not prevented by rapamycin. FoxO3 controls the transcription of autophagy-related genes, including LC3 and Bnip3, and Bnip3 appears to mediate the effect of FoxO3 on autophagy. This effect is not prevented by proteasome inhibitors. Thus, FoxO3 controls the two major systems of protein breakdown in skeletal muscle, the ubiquitin-proteasomal and autophagic/lysosomal pathways, independently. These findings point to FoxO3 and Bnip3 as potential therapeutic targets in muscle wasting disorders and other degenerative and neoplastic diseases in which autophagy is involved.
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FoxO family transcription factors (FoxO1, FoxO3, FoxO4) are critical mediators of the catabolic response during atrophy.
“FoxO family of transcription factors (FoxO1, FoxO3, and FoxO4) are critical mediators of the catabolic response during atrophy [9, 15, 16].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [15]
Activation of mitophagy triggered by transient overexpression of BNIP3 and BNIP3L induces muscle atrophy.
“The activation of mitophagy triggered by the transient overexpression of BNIP3 and BNIP3L induce muscle atrophy [15, 152].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [15]
Transient inhibition of BNIP3 in skeletal muscle partially protects from muscle loss induced by fasting, FoxO3, and FGF21 overexpression.
“In agreement, transient inhibition of BNIP3 in skeletal muscle partially protects from muscle loss induced by fasting, FoxO3, and FGF21 overexpression [15, 152, 212].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [15]
The autophagy lysosomal system is essential for muscle homeostasis.
“we focused in the other muscle major degradative pathway, the autophagy lysosomal system, which is essential for muscle homeostasis.38, 39”
From Fibroblast growth factor 21 controls mitophagy and muscle mass (2019) · cites this paper as [38]
Bnip3 inhibition reduces autophagosome formation and protects against muscle loss during atrophy.
“we already demonstrated that Bnip3 inhibition reduces autophagosome formation and protects against muscle loss during atrophy,25, 38”
From Fibroblast growth factor 21 controls mitophagy and muscle mass (2019) · cites this paper as [38]
Starvation-related atrophy is associated with upregulated autophagy, which is controlled by FOXO3 and is independent of MTOR activity.
“Starvation-related atrophy is also associated with upregulated autophagy, which in turn is controlled by the transcription factor FOXO3 and is independent of MTOR activity [473].”
From Autophagy and ALS: mechanistic insights and therapeutic implications (2022) · cites this paper as [473]
Autophagy is critical for maintaining normal homeostasis of muscle mass in physiological and pathological conditions.
“autophagy is critical for maintaining normal homeostasis of muscle mass in physiological and pathological conditions30,47–49.”
From Disuse-associated loss of the protease Lonp1 in muscle impairs mitochondrial function and causes reduced skeletal muscle mass and strength (2022) · cites this paper as [30]
Excessive activation of autophagy aggravates muscle wasting by removing portion of cytoplasm, proteins, and organelles.
“Excessive activation of autophagy aggravates muscle wasting by removing portion of cytoplasm, proteins, and organelles30,50,51”
From Disuse-associated loss of the protease Lonp1 in muscle impairs mitochondrial function and causes reduced skeletal muscle mass and strength (2022) · cites this paper as [30]
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“which in turn is controlled by the transcription factor FOXO3 and is independent of MTOR activity [473].”
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Self-citation
- Authors
- Mammucari, C., Milan, G., Romanello, V., Masiero, E., Rudolf, R., Del Piccolo, P., Burden, S. J., Di Lisi, R., Sandri, C., Zhao, J., Goldberg, A. L., Schiaffino, S., & Sandri, M.
- Affiliations
- University of Padua (IT)
- Veneto Institute of Molecular Medicine (IT)
- New York University (US)
- Harvard University (US)
- Corresponding author
- Sandri, Marco
- ORCID
- Venue
- Cell Metabolism
- Publisher
- Elsevier BV
- Published
- 2007-12
- Volume
- 6
- Issue
- 6
- Pages
- 458-471
- ISSN
- 1550-4131 (ISSN-L)
- OpenAlex
- W2025192214
- Cited by
- 1,953
- References
- 42
- Citations by year
- 2026: 54 · 2025: 76 · 2024: 88 · 2023: 82 · 2022: 114 · 2021: 127 · 2020: 111 · 2019: 128 · 2018: 119 · 2017: 127 · 2016: 123 · 2015: 124 · 2014: 123 · 2013: 142 · 2012: 118
- FWCI
- 47.27
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell Metabolism (publishedVersion)
- PubMed (publishedVersion)
- Padua Research Archive (University of Padova) (submittedVersion)
- Funders
- National Institute of Neurological Disorders and Stroke (NS27963, R01NS027963)
- National Institute of Arthritis and Musculoskeletal and Skin Diseases (R01AR055255, R01AR055027)
- Topics
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › FOXO transcription factor regulation
- Keywords
- FOXO3, autophagy, skeletal muscle, Akt signaling, BNIP3, LC3, muscle atrophy, protein degradation, transcriptional regulation, rapamycin
- MeSH terms
- Forkhead Box Protein O3, Animals, Autophagy, Gene Expression Regulation, Lysosomes, Membrane Proteins, Mice, Transgenic, Microtubule-Associated Proteins, Models, Biological, Muscular Atrophy, Protein Kinases, Muscle, Skeletal, Mitochondrial Proteins, Ubiquitin, RNA Interference, Proteasome Endopeptidase Complex, Proto-Oncogene Proteins c-akt, Mice, Forkhead Transcription Factors, TOR Serine-Threonine Kinases
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