SIRT3 deacetylates mitochondrial 3-hydroxy-3-methylglutaryl CoA synthase 2 and regulates ketone body production
Open accessAbstract
The mitochondrial sirtuin SIRT3 regulates metabolic homeostasis during fasting and calorie restriction. We identified mitochondrial 3-hydroxy-3-methylglutaryl CoA synthase 2 (HMGCS2) as an acetylated protein and a possible target of SIRT3 in a proteomics survey in hepatic mitochondria from Sirt3(-/-) (SIRT3KO) mice. HMGCS2 is the rate-limiting step in β-hydroxybutyrate synthesis and is hyperacetylated at lysines 310, 447, and 473 in the absence of SIRT3. HMGCS2 is deacetylated by SIRT3 in response to fasting in wild-type mice, but not in SIRT3KO mice. HMGCS2 is deacetylated in vitro when incubated with SIRT3 and in vivo by overexpression of SIRT3. Deacetylation of HMGCS2 lysines 310, 447, and 473 by incubation with wild-type SIRT3 or by mutation to arginine enhances its enzymatic activity. Molecular dynamics simulations show that in silico deacetylation of these three lysines causes conformational changes of HMGCS2 near the active site. Mice lacking SIRT3 show decreased β-hydroxybutyrate levels during fasting. Our findings show SIRT3 regulates ketone body production during fasting and provide molecular insight into how protein acetylation can regulate enzymatic activity.
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Mice lacking SIRT3 or SIRT5 have reduced levels of ketone bodies upon fasting, supporting a positive role for sirtuins in regulating ketone body biosynthesis.
“Mice lacking SIRT3 or SIRT5 have reduced levels of ketone bodies upon fasting, supporting a positive role for sirtuins in regulating ketone body biosynthesis ((Shimazu et al. 2010))((Rardin, He, et al. 2013)).”
From The Mitochondrial Acylome Emerges: Proteomics, Regulation by Sirtuins, and Metabolic and Disease Implications (2018) · cites this paper as Shimazu et al. 2010
SIRT3 deacetylates HMGCS2 at lysines 310, 447, and 473.
“SIRT3 deacetylates HMGCS2 at lysines 310, 447, and 473 ((Shimazu et al. 2010)).”
From The Mitochondrial Acylome Emerges: Proteomics, Regulation by Sirtuins, and Metabolic and Disease Implications (2018) · cites this paper as Shimazu et al. 2010
Mutation of HMGCS2 lysines 310, 447, and 473 to arginines enhances HMGCS2 enzymatic activity.
“In agreement with this model, mutation of these lysines to arginines, which prevent acetylation, enhance HMGCS2 enzymatic activity ((Shimazu et al. 2010)).”
From The Mitochondrial Acylome Emerges: Proteomics, Regulation by Sirtuins, and Metabolic and Disease Implications (2018) · cites this paper as Shimazu et al. 2010
SIRT3 and SIRT5 both positively regulate HMGCS2 activity via deacetylation and desuccinylation, respectively.
“SIRT3 and SIRT5 both positively regulate HMGCS2 activity via respectively deacetylating and desuccinylating it ((Shimazu et al. 2010))((Rardin, He, et al. 2013)).”
From The Mitochondrial Acylome Emerges: Proteomics, Regulation by Sirtuins, and Metabolic and Disease Implications (2018) · cites this paper as Shimazu et al. 2010
In silico deacetylation of HMGCS2 lysines 310, 447, and 473 causes conformational changes near the catalytic site, suggesting acetylation might interfere with enzymatic activity via changing conformation.
“Structural simulations show that in silico deacetylation of these three lysines causes conformational changes of HMGCS2 near the catalytic site, suggesting acetylation might interfere with the enzymatic activity via changing its conformation ((Shimazu et al. 2010)).”
From The Mitochondrial Acylome Emerges: Proteomics, Regulation by Sirtuins, and Metabolic and Disease Implications (2018) · cites this paper as Shimazu et al. 2010
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Cites
Comparison of simple potential functions for simulating liquid water
Jorgensen, W. L., Chandrasekhar, J., Madura, J., Impey, R., & Klein, M. (1983) · The Journal of Chemical Physics · doi:10.1063/1.445869 · Cited by 38,335 · see citing works
Particle mesh Ewald: An N⋅log(N) method for Ewald sums in large systems
Darden, T., York, D., & Pedersen, L. (1993) · The Journal of Chemical Physics · doi:10.1063/1.464397 · Cited by 29,588 · see citing works
Ryckaert, J., Ciccotti, G., & Berendsen, H. (1977) · Journal of Computational Physics · doi:10.1016/0021-9991(77)90098-5 · Cited by 19,525 · see citing works
Cox, J., & Mann, M. (2008) · Nature Biotechnology · doi:10.1038/nbt.1511 · Cited by 14,855 · see citing works
Duan, Y., Wu, C., Chowdhury, S., Lee, M. C., Xiong, G., Zhang, W., Yang, R., Cieplak, P., Luo, R., Lee, T.-S., et al. (2003) · Journal of Computational Chemistry · doi:10.1002/jcc.10349 · Cited by 4,271 · see citing works
Global Survey of Phosphotyrosine Signaling Identifies Oncogenic Kinases in Lung Cancer
Rikova, K., Guo, A., Zeng, Q., Possemato, A., Yu, J., Haack, H., Nardone, J., Lee, K., Reeves, C., Li, Y., et al. (2007) · Cell · doi:10.1016/j.cell.2007.11.025 · Cited by 2,317 · see citing works
Self-citationRegulation of cellular metabolism by protein lysine acetylation
Zhao, S., Xu, W., Jiang, W., Yu, W., Lin, Y., Zhang, T., Yao, J., Zhou, L., Zeng, Y., Li, H., et al. (2010) · Science · doi:10.1126/science.1179689 · Cited by 1,910 · see citing works
Self-citationSIRT3 regulates mitochondrial fatty-acid oxidation by reversible enzyme deacetylation
Hirschey, M. D., Shimazu, T., Goetzman, E., Jing, E., Schwer, B., Lombard, D. B., Grueter, C. A., Harris, C., Biddinger, S., Ilkayeva, O. R., et al. (2010) · Nature · doi:10.1038/nature08778 · Cited by 1,687 · see citing works
Self-citationRegulation of hepatic fatty acid oxidation and ketone body production
McGarry, J. D., & Foster, D. W. (1980) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.49.070180.002143 · Cited by 1,460 · cited 1× · see citing works
“654 Cell Metabolism 12, 654–661, December 1, 2010 a2010 Elsevier tion from the fed to the fasted state, carbohydrate utilization and fatty acid synthesis cease in the liver, and fatty acid oxidation and ketogenesis are induced (McGarry and Foster, 1980).”
BackgroundA role for the mitochondrial deacetylase Sirt3 in regulating energy homeostasis
Ahn, B.-H., Kim, H.-S., Song, S., Lee, I. H., Liu, J., Vassilopoulos, A., Deng, C.-X., & Finkel, T. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0803790105 · Cited by 1,291 · see citing works
Mammalian Sir2 homolog SIRT3 regulates global mitochondrial lysine acetylation
Lombard, D. B., Alt, F. W., Cheng, H.-L., Bunkenborg, J., Streeper, R. S., Mostoslavsky, R., Kim, J., Yancopoulos, G., Valenzuela, D., Murphy, A., et al. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.01636-07 · Cited by 1,216 · see citing works
Self-citationImmunoaffinity profiling of tyrosine phosphorylation in cancer cells
Rush, A. J., Moritz, A., Lee, K. A., Guo, A., Goss, V. L., Spek, E. J., Zhang, H., Zha, X., Polakiewicz, R. D., & Comb, M. J. (2004) · Nature Biotechnology · doi:10.1038/nbt1046 · Cited by 1,126 · see citing works
Acetylation of Metabolic Enzymes Coordinates Carbon Source Utilization and Metabolic Flux
Wang, Q., Zhang, Y., Yang, C., Xiong, H., Lin, Y., Yao, J., Li, H., Xie, L., Zhao, W., Yao, Y., et al. (2010) · Science · doi:10.1126/science.1179687 · Cited by 1,008 · see citing works
Sirtuins deacetylate and activate mammalian acetyl-CoA synthetases
Hallows, W. C., Lee, S., & Denu, J. M. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0604392103 · Cited by 792 · see citing works
Self-citationShi, T., Wang, F., Stieren, E., & Tong, Q. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m414670200 · Cited by 712 · see citing works
Schwer, B., Bunkenborg, J., Verdin, R. O., Andersen, J. S., & Verdin, E. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0603968103 · Cited by 705 · see citing works
Self-citationStructural Basis for Control by Phosphorylation
Johnson, L. N., & Lewis, R. J. (2001) · Chemical Reviews · doi:10.1021/cr000225s · Cited by 643 · see citing works
Cre-lox-regulated conditional RNA interference from transgenes
Ventura, A., Meissner, A., Dillon, C. P., McManus, M. T., Sharp, P. A., Parijs, L. V., Jaenisch, R., & Jacks, T. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0403954101 · Cited by 623 · see citing works
An, J., Muoio, D. M., Shiota, M., Fujimoto, Y., Cline, G. W., Shulman, G. I., Koves, T. R., Stevens, R., Millington, D., & Newgard, C. B. (2004) · Nature Medicine · doi:10.1038/nm995 · Cited by 450 · see citing works
Mitochondrial 3-hydroxy-3-methylglutaryl-CoA synthase: a control enzyme in ketogenesis
Hegardt, F. G. (1999) · Biochemical Journal · doi:10.1042/bj3380569 · Cited by 375 · see citing works
Lee, M. C., & Duan, Y. (2004) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.10470 · Cited by 275 · see citing works
MSQuant, an Open Source Platform for Mass Spectrometry-Based Quantitative Proteomics
Mortensen, P., Gouw, J. W., Olsen, J. V., Ong, S., Rigbolt, K. T. G., Bunkenborg, J., Cox, J., Foster, L. J., Heck, A. J. R., Blagoev, B., et al. (2009) · Journal of Proteome Research · doi:10.1021/pr900721e · Cited by 254 · see citing works
Self-citationKostiuk, M. A., Corvi, M. M., Keller, B. O., Plummer, G. J., Prescher, J. A., Hangauer, M. J., Bertozzi, C. R., Rajaiah, G., Falck, J. R., & Berthiaume, L. G. (2007) · The FASEB Journal · doi:10.1096/fj.07-9199com · Cited by 146 · see citing works
Srivastava, J., Barreiro, G., Groscurth, S., Gingras, A. R., Goult, B. T., Critchley, D. R., Kelly, M. J. S., Jacobson, M. P., & Barber, D. L. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0805163105 · Cited by 138 · see citing works
Self-citationStrengths of Hydrogen Bonds Involving Phosphorylated Amino Acid Side Chains
Mandell, D. J., Chorny, I., Groban, E. S., Wong, S., Levine, E., Rapp, C. S., & Jacobson, M. P. (2007) · Journal of the American Chemical Society · doi:10.1021/ja063019w · Cited by 135 · see citing works
Self-citationFasting-Induced Hypothermia and Reduced Energy Production in Mice Lacking Acetyl-CoA Synthetase 2
Sakakibara, I., Fujino, T., Ishii, M., Tanaka, T., Shimosawa, T., Miura, S., Zhang, W., Tokutake, Y., Yamamoto, J., Awano, M., et al. (2009) · Cell Metabolism · doi:10.1016/j.cmet.2008.12.008 · Cited by 113 · see citing works
Wu, J.-Y., Kao, H., Li, S., Stevens, R., Hillman, S. L., Millington, D. S., & Chen, Y.-T. (2004) · Journal of Clinical Investigation · doi:10.1172/jci19574 · Cited by 104 · see citing works
R.E.DD.B.: A database for RESP and ESP atomic charges, and force field libraries
Dupradeau, F., Cézard, C., Lelong, R., et al. (2007) · Nucleic Acids Research · doi:10.1093/nar/gkm887 · Cited by 102 · see citing works
Quant, P. A., Tubbs, P. K., & Brand, M. D. (1990) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1990.tb15291.x · Cited by 87 · see citing works
Computational studies of protein regulation by post-translational phosphorylation
Narayanan, A., & Jacobson, M. P. (2009) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2009.02.007 · Cited by 81 · see citing works
Self-citationMiziorko, H. M., & Lane, M. D. (1977) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)40672-7 · Cited by 74 · see citing works
Chapter 8 Acetylation of Mitochondrial Proteins
Hirschey, M. D., Shimazu, T., Huang, J., & Verdin, E. (2009) · Methods in Enzymology · doi:10.1016/s0076-6879(09)05008-3 · Cited by 55 · see citing works
Self-citationLowe, D. M., & Tubbs, P. K. (1985) · Biochemical Journal · doi:10.1042/bj2270591 · Cited by 42 · see citing works
Liu, H., & Duan, Y. (2008) · Biophysical Journal · doi:10.1529/biophysj.107.115824 · Cited by 37 · see citing works
Zhu, K., Shirts, M. R., Friesner, R. A., et al. (2007) · Journal of Chemical Theory and Computation · doi:10.1021/ct600129f · Cited by 31 · see citing works
Skaff, D. A., & Miziorko, H. M. (2009) · Analytical Biochemistry · doi:10.1016/j.ab.2009.08.030 · Cited by 29 · see citing works
Laffel (1999) · doi:10.1002/(sici)1520-7560(199911/12)15:6
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Houtkooper, R. H., Pirinen, E., & Auwerx, J. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3293 · Cited by 2,008 · see citing works
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Newman, J. C., & Verdin, E. (2014) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2013.09.002 · Cited by 966 · see citing works
Self-citationCamacho-Pereira, J., Tarragó, M. G., Chini, C. C. S., Nin, V., Escande, C., Warner, G. M., Puranik, A. S., Schoon, R. A., Reid, J. M., Galina, A., et al. (2016) · Cell Metabolism · doi:10.1016/j.cmet.2016.05.006 · Cited by 901 · see citing works
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Newman, J. C., & Verdin, E. (2017) · Annual Review of Nutrition · doi:10.1146/annurev-nutr-071816-064916 · Cited by 872 · see citing works
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Rajman, L., Chwalek, K., & Sinclair, D. A. (2018) · Cell Metabolism · doi:10.1016/j.cmet.2018.02.011 · Cited by 865 · see citing works
Hirschey, M. D., Shimazu, T., Jing, E., Grueter, C. A., Collins, A. M., Aouizerat, B., Stančáková, A., Goetzman, E., Lam, M. M., Schwer, B., et al. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.07.019 · Cited by 787 · see citing works
Self-citationCalorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome
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., et al. (2013) · Molecular Cell · doi:10.1016/j.molcel.2012.10.024 · Cited by 636 · see citing works
Self-citationNishida, Y., Rardin, M. J., Carrico, C., He, W., Sahu, A. K., Gut, P., Najjar, R., Fitch, M., Hellerstein, M., Gibson, B. W., et al. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.05.022 · Cited by 481 · see citing works
Self-citationSirtuins, a promising target in slowing down the ageing process
Grabowska, W., Sikora, E., & Bielak-Zmijewska, A. (2017) · Biogerontology · doi:10.1007/s10522-017-9685-9 · Cited by 470 · see citing works
Martinez-Outschoorn, U. E., Lisanti, M. P., & Sotgia, F. (2014) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2014.01.005 · Cited by 423 · see citing works
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Menzies, K. J., Zhang, H., Katsyuba, E., & Auwerx, J. (2016) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2015.181 · Cited by 331 · see citing works
Carrico, C., Meyer, J. G., He, W., Gibson, B. W., & Verdin, E. (2018) · Cell Metabolism · doi:10.1016/j.cmet.2018.01.016 · Cited by 331 · see citing works
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Marcheva, B., Ramsey, K. M., Peek, C. B., Affinati, A., Maury, E., & Bass, J. (2013) · Handbook of Experimental Pharmacology · doi:10.1007/978-3-642-25950-0_6 · Cited by 282 · see citing works
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Still, A. J., Floyd, B. J., Hebert, A. S., Bingman, C. A., Carson, J. J., Gunderson, D. R., Dolan, B. K., Grimsrud, P. A., Dittenhafer-Reed, K. E., Stapleton, D. S., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.483396 · Cited by 123 · see citing works
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- Authors
- Shimazu, T., Hirschey, M. D., Hua, L., Dittenhafer-Reed, K. E., Schwer, B., Lombard, D. B., Li, Y., Bunkenborg, J., Alt, F. W., Denu, J. M., Jacobson, M. P., & Verdin, E.
- Affiliations
- Gladstone Institutes (US)
- University of California, San Francisco (US)
- Howard Hughes Medical Institute (US)
- Cell Signaling Technology (United States) (US)
- University of Southern Denmark (DK)
- University of Wisconsin–Madison (US)
- Corresponding author
- Verdin, Eric
- ORCID
- Venue
- Cell Metabolism
- Publisher
- Elsevier BV
- Published
- 2010-12
- Volume
- 12
- Issue
- 6
- Pages
- 654-661
- ISSN
- 1550-4131 (ISSN-L)
- PMC
- PMC3310379
- OpenAlex
- W2100476416
- Cited by
- 484
- References
- 37
- Citations by year
- 2026: 16 · 2025: 24 · 2024: 17 · 2023: 28 · 2022: 36 · 2021: 38 · 2020: 27 · 2019: 21 · 2018: 32 · 2017: 37 · 2016: 39 · 2015: 21 · 2014: 38 · 2013: 44 · 2012: 46
- FWCI
- 14.08
- 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, 959 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
- Cell Metabolism (publishedVersion)
- PubMed (publishedVersion)
- University of Southern Denmark Research Portal (University of Southern Denmark) (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Science Foundation (AG022325)
- National Institutes of Health (GM-065386, GM-081710)
- National Center for Research Resources (RR18928-01)
- Ellison Medical Foundation
- Topics
- Health Sciences › Medicine › Geriatrics and Gerontology › Sirtuins and Resveratrol in Medicine
- Health Sciences › Medicine › Physiology › Adipose Tissue and Metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Cancer, Lipids, and Metabolism
- Keywords
- SIRT3, HMGCS2, protein deacetylation, protein acetylation, ketone synthesis, beta-hydroxybutyrate, fasting, mitochondrial metabolism, liver mitochondria, lysine acetylation, enzyme conformational change, molecular dynamics simulation, SIRT3 knockout mice
- MeSH terms
- Acetylation, Animals, Fasting, Hydroxymethylglutaryl-CoA Synthase, Ketone Bodies, Liver, Mitochondria, Mass Spectrometry, Immunoblotting, Mice, Knockout, Immunoprecipitation, Mice, Molecular Dynamics Simulation, Sirtuin 3
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