Sirt3 promotes the urea cycle and fatty acid oxidation during dietary restriction
Open accessAbstract
Emerging evidence suggests that protein acetylation is a broad-ranging regulatory mechanism. Here we utilize acetyl-peptide arrays and metabolomic analyses to identify substrates of mitochondrial deacetylase Sirt3. We identified ornithine transcarbamoylase (OTC) from the urea cycle, and enzymes involved in β-oxidation. Metabolomic analyses of fasted mice lacking Sirt3 (sirt3(-/-)) revealed alterations in β-oxidation and the urea cycle. Biochemical analysis demonstrated that Sirt3 directly deacetylates OTC and stimulates its activity. Mice under caloric restriction (CR) increased Sirt3 protein levels, leading to deacetylation and stimulation of OTC activity. In contrast, sirt3(-/-) mice failed to deacetylate OTC in response to CR. Inability to stimulate OTC under CR led to a failure to reduce orotic acid levels, a known outcome of OTC deficiency. Thus, Sirt3 directly regulates OTC activity and promotes the urea cycle during CR, and the results suggest that under low energy input, Sirt3 modulates mitochondria by promoting amino acid catabolism and β-oxidation.
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SIRT3 deacetylates OTC at lysine 88.
“It targets the other mitochondrial enzyme, ornithine transcarboxylase (OTC), by deacetylation of lysine 88 ((Hallows et al. 2011)).”
From The Mitochondrial Acylome Emerges: Proteomics, Regulation by Sirtuins, and Metabolic and Disease Implications (2018) · cites this paper as Hallows et al. 2011
Calorie restriction stimulates the urea cycle and upregulates OTC activity; this upregulation is lost in the absence of SIRT3, leading to increased orotic acid levels.
“Calorie restriction stimulates the urea cycle and up-regulates OTC activity; this up-regulation of OTC activity is lost in the absence of SIRT3, leading to increased orotic acid levels, a known outcome of OTC deficiency ((Hallows et al. 2011)).”
From The Mitochondrial Acylome Emerges: Proteomics, Regulation by Sirtuins, and Metabolic and Disease Implications (2018) · cites this paper as Hallows et al. 2011
Metabolomic analysis of fasted mice lacking SIRT3 shows metabolite alterations in the urea cycle.
“Metabolomic analysis of fasted mice lacking SIRT3 shows metabolite alterations in the urea cycle ((Hallows et al. 2011)).”
From The Mitochondrial Acylome Emerges: Proteomics, Regulation by Sirtuins, and Metabolic and Disease Implications (2018) · cites this paper as Hallows et al. 2011
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- Authors
- Hallows, W. C., Yu, W., Smith, B. C., Devires, M. K., Ellinger, J. J., Someya, S., Shortreed, M. R., Prolla, T., Markley, J. L., Smith, L. M., Zhao, S., Guan, K.-L., & Denu, J. M.
- Affiliations
- University of Wisconsin–Madison (US)
- Fudan University (CN)
- Corresponding author
- Denu, John M.
- ORCID
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2011-01
- Volume
- 41
- Issue
- 2
- Pages
- 139-149
- ISSN
- 1097-2765 (ISSN-L)
- PMC
- PMC3101115
- OpenAlex
- W2084481577
- Cited by
- 389
- References
- 46
- Citations by year
- 2026: 4 · 2025: 21 · 2024: 11 · 2023: 16 · 2022: 20 · 2021: 25 · 2020: 14 · 2019: 26 · 2018: 39 · 2017: 28 · 2016: 27 · 2015: 33 · 2014: 26 · 2013: 33 · 2012: 47
- FWCI
- 19.06
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Molecular Cell (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- University of Wisconsin-Madison
- National Institutes of Health
- National Institute on Aging (P30AG028740)
- National Cancer Institute (R01CA108941)
- National Institute on Deafness and Other Communication Disorders (R03DC011840)
- National Institute of General Medical Sciences (P41 GM 66326, GM-065386, R01GM065386, P41GM066326)
- National Center for Research Resources (P41RR002301, P41-RR02301)
- Topics
- Health Sciences › Medicine › Geriatrics and Gerontology › Sirtuins and Resveratrol in Medicine
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Molecular Research
- Keywords
- SIRT3, protein acetylation, ornithine transcarbamylase, urea cycle, fatty acid beta-oxidation, caloric restriction, dietary restriction, mitochondrial deacetylase, orotic acid, amino acid catabolism, SIRT3 knockout mice
- MeSH terms
- Acetylation, Animals, Energy Metabolism, Fatty Acids, Humans, Liver, Mice, Inbred Strains, Mitochondria, Ornithine Carbamoyltransferase, Oxidation-Reduction, Urea, Caloric Restriction, Mice, Sirtuin 3, HEK293 Cells
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