Foxk proteins repress the initiation of starvation-induced atrophy and autophagy programs
Open accessAbstract
Autophagy is the primary catabolic process triggered in response to starvation. Although autophagic regulation within the cytosolic compartment is well established, it is becoming clear that nuclear events also regulate the induction or repression of autophagy. Nevertheless, a thorough understanding of the mechanisms by which sequence-specific transcription factors modulate expression of genes required for autophagy is lacking. Here, we identify Foxk proteins (Foxk1 and Foxk2) as transcriptional repressors of autophagy in muscle cells and fibroblasts. Interestingly, Foxk1/2 serve to counter-balance another forkhead transcription factor, Foxo3, which induces an overlapping set of autophagic and atrophic targets in muscle. Foxk1/2 specifically recruits Sin3A-HDAC complexes to restrict acetylation of histone H4 and expression of critical autophagy genes. Remarkably, mTOR promotes the transcriptional activity of Foxk1 by facilitating nuclear entry to specifically limit basal levels of autophagy in nutrient-rich conditions. Our study highlights an ancient, conserved mechanism whereby nutritional status is interpreted by mTOR to restrict autophagy by repressing essential autophagy genes through Foxk-Sin3-mediated transcriptional control.
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When nutrients are available, mTORC1 promotes nuclear relocalization of Foxk, which binds to promoters of autophagy genes, recruits Sin3A-HDAC complex, and compacts chromatin, preventing FoxO3 recruitment.
“When nutrients are available, the mTORC1 complex promotes nuclear relocalization of Foxk, which binds to the promoters of autophagy genes, recruits the Sin3A-HDAC complex, and compacts chromatin, therefore preventing FoxO3 recruitment.”
From Mechanisms of muscle atrophy and hypertrophy: implications in health and disease (2021) · cites this paper as [81]
In the absence of nutrients, Foxk is in cytosol allowing FoxO3-dependent transcription of autophagy genes.
“In the absence of nutrients, Foxk is in cytosol allowing FoxO3-dependent transcription of autophagy genes81.”
From Mechanisms of muscle atrophy and hypertrophy: implications in health and disease (2021) · cites this paper as [81]
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- Authors
- Bowman, C. J., Ayer, D. E., & Dynlacht, B. D.
- Affiliations
- New York University (US)
- University of Utah (US)
- Corresponding author
- Dynlacht, Brian David
- Venue
- Nature Cell Biology
- Published
- 2014-11-17
- Volume
- 16
- Issue
- 12
- Pages
- 1202-1214
- ISSN
- 1465-7392 (ISSN-L)
- 1476-4679
- PMC
- PMC4250422
- OpenAlex
- W2047791731
- Cited by
- 153
- References
- 67
- Citations by year
- 2026: 8 · 2025: 18 · 2024: 15 · 2023: 18 · 2022: 18 · 2021: 9 · 2020: 15 · 2019: 13 · 2018: 10 · 2017: 10 · 2016: 11 · 2015: 8
- FWCI
- 7.30
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- NYU Langone Medical Center
- National Institutes of Health (5r01gm055668-17)
- National Institute on Aging (F30AG040894)
- National Cancer Institute (R01CA077245, P30CA016087)
- National Institute of General Medical Sciences (R01GM067132, R01-GM055668)
- 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
- FOXK1, FOXK2, FOXO3, autophagy, muscle atrophy, starvation, transcriptional repression, histone H4 acetylation, mTOR, nuclear translocation, muscle cells, fibroblasts, nutritional status
- MeSH terms
- Forkhead Box Protein O3, Acetylation, Animals, Autophagy, Binding Sites, Cell Line, Fibroblasts, Histone Deacetylases, Histones, Nutritional Status, Promoter Regions, Genetic, Protein Binding, Repressor Proteins, Signal Transduction, Transcriptional Activation, Myoblasts, RNA Interference, RNA, Small Interfering, Mice, Forkhead Transcription Factors, Sin3 Histone Deacetylase and Corepressor Complex, TOR Serine-Threonine Kinases
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