Cited by 258Cancer, Lipids, and MetabolismAdvanced Proteomics Techniques and ApplicationsRedox biology and oxidative stress

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A Class of Reactive Acyl-CoA Species Reveals the Non-enzymatic Origins of Protein Acylation

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Wagner, Gregory R., Bhatt, Dhaval P., O’Connell, Thomas M., Thompson, J. Will, Dubois, Laura G., Backos, Donald S., Yang, Hao, Mitchell, Grant A., Ilkayeva, Olga R., Stevens, Robert D., Grimsrud, Paul A., Hirschey, Matthew D.·2017·Cell Metabolism

DOI 10.1016/j.cmet.2017.03.006PMC PMC5399522

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Abstract

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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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: Bhatt, Dhaval P.
O’Connell, Thomas M.
Thompson, J. Will
Dubois, Laura G.
Backos, Donald S.
Yang, Hao
Mitchell, Grant A.
Ilkayeva, Olga R.
Stevens, Robert D.
Grimsrud, Paul A.
Hirschey, Matthew D.
Venue: Cell Metabolism
Publisher: Elsevier BV
Published: 2017-04
Volume: 25
Issue: 4
Pages: 823-837.e8
ISSN: 1550-4131 (ISSN-L)
DOI: 10.1016/j.cmet.2017.03.006
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: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 368 d)
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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A Class of Reactive Acyl-CoA Species Reveals the Non-enzymatic Origins of Protein Acylation

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