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A Class of Reactive Acyl-CoA Species Reveals the Non-enzymatic Origins of Protein Acylation
Open accessAbstract
The mechanisms underlying the formation of acyl protein modifications remain poorly understood. By investigating the reactivity of endogenous acyl-CoA metabolites, we found a class of acyl-CoAs that undergo intramolecular catalysis to form reactive intermediates that non-enzymatically modify proteins. Based on this mechanism, we predicted, validated, and characterized a protein modification: 3-hydroxy-3-methylglutaryl(HMG)-lysine. In a model of altered HMG-CoA metabolism, we found evidence of two additional protein modifications: 3-methylglutaconyl(MGc)-lysine and 3-methylglutaryl(MG)-lysine. Using quantitative proteomics, we compared the "acylomes" of two reactive acyl-CoA species, namely HMG-CoA and glutaryl-CoA, which are generated in different pathways. We found proteins that are uniquely modified by each reactive metabolite, as well as common proteins and pathways. We identified the tricarboxylic acid cycle as a pathway commonly regulated by acylation and validated malate dehydrogenase as a key target. These data uncover a fundamental relationship between reactive acyl-CoA species and proteins and define a new regulatory paradigm in metabolism.
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“Divalent acyl groups such as succinyl- and glutaryl-CoA can use this alternative non-enzymatic reaction mechanism to achieve higher reaction rates than monovalent acyl species such as acetyl-CoA.”
From The Mitochondrial Acylome Emerges: Proteomics, Regulation by Sirtuins, and Metabolic and Disease Implications (2018) · cites this paper as Wagner et al. 2017
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“Recent work has further shown that some acyl-CoA species can modify lysines via a cyclic anhydride intermediate (Wagner et al. 2017).”
From The Mitochondrial Acylome Emerges: Proteomics, Regulation by Sirtuins, and Metabolic and Disease Implications (2018) · cites this paper as Wagner et al. 2017
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López-Otín, C., Blasco, M. A., Partridge, L., Serrano, M., & Kroemer, G. (2013) · Cell · doi:10.1016/j.cell.2013.05.039 · Cited by 14,982
CHARMM: The biomolecular simulation program
Brooks, B. R., Brooks, C. L., MacKerell, A. D., Nilsson, L., Petrella, R. J., Roux, B., Won, Y., Archontis, G., Bartels, C., Boresch, S., et al. (2009) · Journal of Computational Chemistry · doi:10.1002/jcc.21287 · Cited by 9,115
Lysine acetylation targets protein complexes and co-regulates major cellular functions
Choudhary, C., Kumar, C., Gnad, F., Nielsen, M. L., Rehman, M., Walther, T. C., Olsen, J. V., & Mann, M. (2009) · Science · doi:10.1126/science.1175371 · Cited by 4,040
PhosphoSitePlus, 2014: mutations, PTMs and recalibrations
Hornbeck, P. V., Zhang, B., Murray, B., Kornhauser, J. M., Latham, V., & Skrzypek, E. (2015) · Nucleic Acids Research · doi:10.1093/nar/gku1267 · Cited by 3,411
Physiological Roles of Mitochondrial Reactive Oxygen Species
Sena, L. A., & Chandel, N. S. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.09.025 · Cited by 2,632
Regulation 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
SIRT3 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
Self-citationSirt5 Is a NAD-Dependent Protein Lysine Demalonylase and Desuccinylase
Du, J., Zhou, Y., Su, X., Yu, J. J., Khan, S., Jiang, H., Kim, J., Woo, J., Kim, J. H., Choi, B. H., et al. (2011) · Science · doi:10.1126/science.1207861 · Cited by 1,429
MitoCarta2.0: an updated inventory of mammalian mitochondrial proteins
Calvo, S. E., Clauser, K. R., & Mootha, V. K. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkv1003 · Cited by 1,251
The Preparation of S-Succinyl Coenzyme A
Simon, E. J., & Shemin, D. (1953) · Journal of the American Chemical Society · doi:10.1021/ja01106a522 · Cited by 1,035
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“Interestingly, our concurrent study demonstrates that reactive acyl-CoA species (RAS) have the potential to react non-enzymatically with lysine residues to generate protein modifications (Wagner et al., 2017).”
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Chiba, T., Peasley, K., Cargill, K. R., Maringer, K. V., Bharathi, S. S., Mukherjee, E., Zhang, Y., Holtz, A. N., Basisty, N., Yagobian, S. D., et al. (2019) · Journal of the American Society of Nephrology · doi:10.1681/asn.2019020163 · Cited by 143
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Pannek, M., Simic, Z., Fuszard, M. A., Meleshin, M., Rotili, D., Mai, A., Schutkowski, M., & Steegborn, C. (2017) · Nature Communications · doi:10.1038/s41467-017-01701-2 · Cited by 103
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Ruan, L., Wang, Y., Zhang, X., Tomaszewski, A., McNamara, J. T., & Li, R. (2020) · Annual Review of Biophysics · doi:10.1146/annurev-biophys-121219-081604 · Cited by 95
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Self-citationWang, Y., Yang, H., Geerts, C., Fürtös, A., Waters, P. J., Cyr, D., Wang, S., & Mitchell, G. A. (2022) · Molecular Genetics and Metabolism · doi:10.1016/j.ymgme.2022.106966 · Cited by 74
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Mericskay, M., Zuurbier, C. J., Heather, L. C., Karlstaedt, A., Inserte, J., Bertrand, L., Kararigas, G., Ruiz‐Meana, M., Maack, C., & Schiattarella, G. G. (2025) · Nature Reviews Cardiology · doi:10.1038/s41569-025-01166-7 · Cited by 68
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Self-citationWang, J., Mao, L., Wang, J., Zhang, X., Wu, M. C., Wen, Q., & Yu, S. (2023) · Cellular Oncology · doi:10.1007/s13402-023-00775-z · Cited by 58
He, X., Wang, Q., Cheng, X., Wang, W., Li, Y., Nan, Y., Wu, J., Xiu, B., Jiang, T., Bergholz, J. S., et al. (2025) · Cell · doi:10.1016/j.cell.2025.01.043 · Cited by 57
Schmiesing, J., Storch, S., Dörfler, A.-C., Schweizer, M., Makrypidi‐Fraune, G., Thelen, M., Sylvester, M., Gieselmann, V., Meyer‐Schwesinger, C., Koch‐Nolte, F., et al. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.08.014 · Cited by 55
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Jones, D. E., Perez, L., & Ryan, R. O. (2019) · Clinica Chimica Acta · doi:10.1016/j.cca.2019.11.006 · Cited by 54
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Teodoro, J. S., Silva, R., Machado, I. F., Rosello, A. P., Roselló‐Catafau, J., Rolo, A. P., & Palmeira, C. M. (2022) · Cells · doi:10.3390/cells11040688 · Cited by 52
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Zou, L., Yang, Y., Wang, Z., Fu, X., He, X., Song, J., Li, T., Ma, H., & Yu, T. (2022) · Aging and Disease · doi:10.14336/ad.2022.0711 · Cited by 54
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Locasale, J. W. (2017) · Current Opinion in Systems Biology · doi:10.1016/j.coisb.2017.11.005 · Cited by 53
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Han, L., Li, J., Li, J., Pan, C., Xiao, Y., Lan, X., & Wang, M. (2020) · Food & Function · doi:10.1039/c9fo02334h · Cited by 52
Head, P. E., Myung, S., Chen, Y., Schneller, J. L., Wang, C., Duncan, N., Hoffman, P., Chang, D., Gebremariam, A., Gucek, M., et al. (2022) · Science Translational Medicine · doi:10.1126/scitranslmed.abn4772 · Cited by 52
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Meyer, J. G., Softic, S., Basisty, N., Rardin, M. J., Verdin, E. M., Gibson, B. W., Ilkayeva, O., Newgard, C. B., Kahn, C. R., & Schilling, B. (2018) · PLoS ONE · doi:10.1371/journal.pone.0208973 · Cited by 52
Self-citationFisher‐Wellman, K. H., Draper, J. A., Davidson, M. T., Williams, A. S., Narowski, T. M., Slentz, D. H., Ilkayeva, O., Stevens, R. D., Wagner, G. R., Najjar, R. S., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.01.057 · Cited by 49
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Weyh, M., Jokisch, M., Nguyen, T., Fottner, M., & Lang, K. (2024) · Nature Chemistry · doi:10.1038/s41557-024-01500-5 · Cited by 49
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Metadata
- Authors
- Wagner, G. R., Bhatt, D. P., O’Connell, T. M., Thompson, J. W., Dubois, L. G., Backos, D. S., Yang, H., Mitchell, G. A., Ilkayeva, O. R., Stevens, R. D., Grimsrud, P. A., & Hirschey, M. D.
- Affiliations
- Duke University (US)
- Duke Medical Center (US)
- University of Colorado Anschutz (US)
- Centre Hospitalier Universitaire Sainte-Justine (CA)
- Corresponding author
- Hirschey, Matthew D.
- ORCID
- Venue
- Cell Metabolism
- Publisher
- Elsevier BV
- Published
- 2017-04
- Volume
- 25
- Issue
- 4
- Pages
- 823-837.e8
- ISSN
- 1550-4131 (ISSN-L)
- PMC
- PMC5399522
- OpenAlex
- W2604275396
- Cited by
- 258
- References
- 48
- Citations by year
- 2026: 21 · 2025: 24 · 2024: 28 · 2023: 24 · 2022: 37 · 2021: 35 · 2020: 28 · 2019: 19 · 2018: 27 · 2017: 15
- FWCI
- 8.17
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell Metabolism (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institute of Diabetes and Digestive and Kidney Diseases (2T32DK007012)
- Ellison Medical Foundation
- American Heart Association (12IRG9010008)
- National Institutes of Health
- Canadian Institutes of Health Research (034368-UNC, 178978)
- National Institute on Alcohol Abuse and Alcoholism (R01AA022146)
- Centre hospitalier régional universitaire de Lille
- National Institute on Aging (P30AG028716-01, R01AG045351)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Cancer, Lipids, and Metabolism
- Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Keywords
- protein acylation, HMG-CoA, glutaryl-CoA, lysine acylation, intramolecular catalysis, TCA cycle, malate dehydrogenase, HMG-CoA reductase inhibition, metabolic regulation
- MeSH terms
- Acyl Coenzyme A, Acylation, Anhydrides, Citric Acid Cycle, Lysine, Mitochondria, Protein Processing, Post-Translational, Proteins, Proteomics, Biocatalysis, Metabolome
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