HDAC1 activates FoxO and is both sufficient and required for skeletal muscle atrophy

Beharry, Adam W.; Sandesara, Pooja B.; Roberts, Brandon M.; Ferreira, Leonardo F.; Senf, Sarah M.; Judge, Andrew R.

doi:10.1242/jcs.136390

Cited by 128Muscle Physiology and DisordersFOXO transcription factor regulationHistone Deacetylase Inhibitors Research

HDAC1 activates FoxO and is both sufficient and required for skeletal muscle atrophy

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Beharry, Adam W., Sandesara, Pooja B., Roberts, Brandon M., Ferreira, Leonardo F., Senf, Sarah M., Judge, Andrew R.·2014·Journal of Cell Science

DOI 10.1242/jcs.136390PMC PMC3970557

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Abstract

The Forkhead boxO (FoxO) transcription factors are activated and necessary for the muscle atrophy during several pathophysiological conditions, including muscle disuse and cancer cachexia. Yet, the mechanisms which lead to FoxO activation are not well defined. Recent data from our lab and others indicate that the activity of FoxO is repressed under basal conditions via reversible lysine acetylation, which becomes compromised during catabolic conditions. The purpose of the current study was therefore to determine the extent to which histone deacetylase (HDAC) proteins contribute to FoxO activation and induction of the muscle atrophy program. Through the use of various pharmacological inhibitors to block HDAC activity we demonstrate that class I HDACs are key regulators of FoxO and the muscle atrophy program during both nutrient deprivation and skeletal muscle disuse. Furthermore, we demonstrate through the use of WT and d.n. HDAC1 expression plasmids that HDAC1 is sufficient to activate FoxO and induce muscle fiber atrophy, in vivo, and is necessary for the muscle fiber atrophy associated with muscle disuse. The ability of HDAC1 to cause muscle atrophy required its deacetylase activity and was linked to its induction of several atrophy genes, including atrogin-1, which required FoxO3a deacetylation. Moreover, pharmacological inhibition of class I HDACs during muscle disuse via treatment with MS-275 significantly attenuated both disuse muscle fiber atrophy and contractile dysfunction. Together these data solidify the importance of class I HDACs in the muscle atrophy program and indicate that class I HDAC inhibitors are feasible countermeasures to impede muscle atrophy and weakness.

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p300/CBP-mediated acetylation inhibits the FoxO3-dependent atrophy program, while HDAC-mediated deacetylation activates FoxOs.
“For instance, p300/CBP-mediated acetylation inhibits FoxO3-dependent atrophy program, while HDAC-mediated deacetylation activates FoxOs65,66.”
From Mechanisms of muscle atrophy and hypertrophy: implications in health and disease (2021) · cites this paper as [65]
HDAC inhibitors have been shown to be successful in blocking FoxO and sparing muscle mass.
“Indeed, HDAC inhibitors have been shown to be successful in blocking FoxO and sparing muscle mass65.”
From Mechanisms of muscle atrophy and hypertrophy: implications in health and disease (2021) · cites this paper as [65]

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Authors: Beharry, A. W., Sandesara, P. B., Roberts, B. M., Ferreira, L. F., Senf, S. M., & Judge, A. R.
Affiliations: University of Florida Health (US)
University of Florida (US)
Corresponding author: Judge, Andrew R.
ORCID: Roberts, Brandon M.
Ferreira, Leonardo F.
Venue: Journal of Cell Science
Publisher: The Company of Biologists
Published: 2014-01-01
Volume: 127
Issue: Pt 7
Pages: 1441-53
ISSN: 0021-9533 (ISSN-L)
1477-9137
DOI: 10.1242/jcs.136390
PMC: PMC3970557
OpenAlex: W2105597626
Cited by: 128
References: 58
Citations by year: 2026: 3 · 2025: 10 · 2024: 11 · 2023: 6 · 2022: 11 · 2021: 17 · 2020: 16 · 2019: 9 · 2018: 7 · 2017: 4 · 2016: 12 · 2015: 18 · 2014: 4
FWCI: 5.20
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Locations: Journal of Cell Science (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
HighWire Press Open Archive (submittedVersion)
Funders: National Institute on Aging (P30AG028740)
National Heart, Lung, and Blood Institute (R00HL098453)
National Institute of Arthritis and Musculoskeletal and Skin Diseases (R01AR060209)
Eunice Kennedy Shriver National Institute of Child Health and Human Development (T32HD043730)
Topics: 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
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Histone Deacetylase Inhibitors Research
Keywords: HDAC1, FOXO, skeletal muscle atrophy, class I histone deacetylases, muscle disuse, nutrient deprivation, atrogin-1, histone deacetylase inhibitors, entinostat, contractile dysfunction, muscle weakness, cancer cachexia
MeSH terms: Acetylation, Animals, Humans, Male, Muscle Proteins, Muscular Atrophy, Protein Processing, Post-Translational, Signal Transduction, Rats, Sprague-Dawley, Muscle, Skeletal, Mice, Rats, Forkhead Transcription Factors, Histone Deacetylase 1

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HDAC1 activates FoxO and is both sufficient and required for skeletal muscle atrophy

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