Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome
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Calorie restriction (CR) extends life span in diverse species. Mitochondria play a key role in CR adaptation; however, the molecular details remain elusive. We developed and applied a quantitative mass spectrometry method to probe the liver mitochondrial acetyl-proteome during CR versus control diet in mice that were wild-type or lacked the protein deacetylase SIRT3. Quantification of 3,285 acetylation sites-2,193 from mitochondrial proteins-rendered a comprehensive atlas of the acetyl-proteome and enabled global site-specific, relative acetyl occupancy measurements between all four experimental conditions. Bioinformatic and biochemical analyses provided additional support for the effects of specific acetylation on mitochondrial protein function. Our results (1) reveal widespread reprogramming of mitochondrial protein acetylation in response to CR and SIRT3, (2) identify three biochemically distinct classes of acetylation sites, and (3) provide evidence that SIRT3 is a prominent regulator in CR adaptation by coordinately deacetylating proteins involved in diverse pathways of metabolism and mitochondrial maintenance.
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During calorie restriction, liver mitochondrial proteins show an overall increase in acetylation, while proteins in other cellular compartments do not.
“Proteomic characterization of the changes in liver reveals a complicated landscape of alterations, but an overall increase in acetylation levels for mitochondrial proteins but not those found in other cellular compartments during CR (Hebert et al. 2013).”
From The Mitochondrial Acylome Emerges: Proteomics, Regulation by Sirtuins, and Metabolic and Disease Implications (2018) · cites this paper as Hebert et al. 2013
SIRT5 has a major role in controlling lysine succinylation, similar to SIRT3's principal role in mitochondrial lysine acetylation.
“Our data are consistent with a major role for SIRT5 in regulating Ksucc levels, which is analogous to the principal role of SIRT3 in regulating mitochondrial Lys acetylation (Hebert et al., 2013; Lombard et al., 2007; Smith et al., 2011).”
From SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways (2013) · cites this paper as Hebert et al., 2013
The global increase in protein acetylation does not reflect how specific residues are deacetylated upon caloric restriction.
“Indeed, the global increase in protein acetylation does not reflect how specific residues are deacetylated upon CR (Hebert et al, 2013).”
From Mitochondrial response to nutrient availability and its role in metabolic disease (2014) · cites this paper as Hebert et al, 2013
Recent evidence points toward a role of the mitochondrial sirtuin SIRT3 in the prevention of age-related diseases, possibly through modulation of the mitochondrial acetyl proteome.
“For instance, recent evidence points toward a role of the mitochondrial sirtuin SIRT3 in the prevention of age-related diseases, possibly through modulation of the mitochondrial acetyl proteome (Hebert et al., 2013).”
From The Search for Antiaging Interventions: From Elixirs to Fasting Regimens (2014) · cites this paper as Hebert et al., 2013
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BackgroundMitochondrial Function, Biology, and Role in Disease
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BackgroundSIRT3 Mediates Multi-Tissue Coupling for Metabolic Fuel Switching
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Self-citation
- Authors
- Hebert, A. S., Dittenhafer-Reed, K. E., Yu, W., Bailey, D. J., Selen, E. S., Boersma, M. D., Carson, J. J., Tonelli, M., Balloon, A. J., Higbee, A. J., Westphall, M. S., Pagliarini, D. J., Prolla, T. A., Assadi-Porter, F., Roy, S., Denu, J. M., & Coon, J. J.
- Affiliations
- University of Wisconsin–Madison (US)
- Corresponding author
- Denu, John M.
- ORCID
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2013-01
- Volume
- 49
- Issue
- 1
- Pages
- 186-199
- ISSN
- 1097-2765 (ISSN-L)
- PMC
- PMC3704155
- OpenAlex
- W2096965531
- Cited by
- 636
- References
- 64
- Citations by year
- 2026: 18 · 2025: 24 · 2024: 26 · 2023: 43 · 2022: 46 · 2021: 57 · 2020: 55 · 2019: 44 · 2018: 49 · 2017: 47 · 2016: 56 · 2015: 63 · 2014: 64 · 2013: 41 · 2012: 1
- FWCI
- 26.30
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- www.elsevier.com/open-access/userlicense/1.0/ (vor, 374 d)
- doi.org/10.15223/policy-017 (stm-asf)
- doi.org/10.15223/policy-037 (stm-asf)
- doi.org/10.15223/policy-012 (stm-asf)
- doi.org/10.15223/policy-029 (stm-asf)
- doi.org/10.15223/policy-004 (stm-asf)
- Locations
- Molecular Cell (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Science Foundation (5T32GM08349)
- National Institutes of Health (GM065386, GM080148, RC1DK086410)
- National Institute on Aging (AG038679)
- Topics
- Health Sciences › Medicine › Geriatrics and Gerontology › Sirtuins and Resveratrol in Medicine
- Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Aging › Genetics, Aging, and Longevity in Model Organisms
- Keywords
- caloric restriction, SIRT3, mitochondrial protein acetylation, acetylome, protein deacetylation, liver mitochondria, longevity, metabolic reprogramming, mitochondrial maintenance
- MeSH terms
- Acetyl Coenzyme A, Acetylation, Adaptation, Physiological, Amino Acid Sequence, Amino Acids, Animals, Cells, Cultured, Chromatography, Ion Exchange, Liver, Mice, Inbred C57BL, Mitochondria, Liver, Molecular Sequence Data, Peptide Fragments, Protein Processing, Post-Translational, Staining and Labeling, Gene Expression, Cluster Analysis, Consensus Sequence, Proteome, Amino Acid Motifs, Mitochondrial Proteins, Caloric Restriction, Genes, Mitochondrial, Carbohydrate Metabolism, Mice, Tandem Mass Spectrometry, Sirtuin 3
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Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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