Adenine Nucleotide Translocase Is Acetylated in Vivo in Human Muscle: Modeling Predicts a Decreased ADP Affinity and Altered Control of Oxidative Phosphorylation
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Proteomics techniques have revealed that lysine acetylation is abundant in mitochondrial proteins. This study was undertaken (1) to determine the relationship between mitochondrial protein acetylation and insulin sensitivity in human skeletal muscle, identifying key acetylated proteins, and (2) to use molecular modeling techniques to understand the functional consequences of acetylation of adenine nucleotide translocase 1 (ANT1), which we found to be abundantly acetylated. Eight lean and eight obese nondiabetic subjects had euglycemic clamps and muscle biopsies for isolation of mitochondrial proteins and proteomics analysis. A number of acetylated mitochondrial proteins were identified in muscle biopsies. Overall, acetylation of mitochondrial proteins was correlated with insulin action (r = 0.60; P < 0.05). Of the acetylated proteins, ANT1, which catalyzes ADP–ATP exchange across the inner mitochondrial membrane, was acetylated at lysines 10, 23, and 92. The extent of acetylation of lysine 23 decreased following exercise, depending on insulin sensitivity. Molecular dynamics modeling and ensemble docking simulations predicted the ADP binding site of ANT1 to be a pocket of positively charged residues, including lysine 23. Calculated ADP–ANT1 binding affinities were physiologically relevant and predicted substantial reductions in affinity upon acetylation of lysine 23. Insertion of these derived binding affinities as parameters into a complete mathematical description of ANT1 kinetics predicted marked reductions in adenine nucleotide flux resulting from acetylation of lysine 23. Therefore, acetylation of ANT1 could have dramatic physiological effects on ADP–ATP exchange. Dysregulation of acetylation of mitochondrial proteins such as ANT1 therefore could be related to changes in mitochondrial function that are associated with insulin resistance.
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ANTs are known to be acetylated, and some acetylation sites are predicted to be functionally important for channel function.
“their partners on the inner membrane, adenine nucleotide translocases (ANTs), are known to be acetylated and some sites are predicted to be functionally important to channel function (Mielke et al. 2014).”
From The Mitochondrial Acylome Emerges: Proteomics, Regulation by Sirtuins, and Metabolic and Disease Implications (2018) · cites this paper as Mielke et al. 2014
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Self-citationRole of Mitochondria in the Skeletal Muscle Metabolism in Obesity and Type 2 Diabetes
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KAT2 paralogs prevent dsRNA accumulation and interferon signaling to maintain intestinal stem cellsPreprint
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Processes and therapeutic perspectives of acylation modifications of lysine and cysteine in tumors
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- Authors
- Mielke, C., Lefort, N., McLean, C. G., Cordova, J. M., Langlais, P. R., Bordner, A. J., Te, J. A., Ozkan, S. B., Willis, W. T., & Mandarino, L. J.
- Affiliations
- Arizona State University (US)
- Mayo Clinic in Arizona (US)
- Corresponding author
- Mandarino, Lawrence J.
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 2014-06-02
- Volume
- 53
- Issue
- 23
- Pages
- 3817-3829
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- PMC
- PMC4067143
- OpenAlex
- W2314015436
- Cited by
- 53
- References
- 44
- Citations by year
- 2026: 2 · 2024: 4 · 2023: 4 · 2022: 10 · 2021: 6 · 2020: 4 · 2019: 6 · 2018: 7 · 2017: 3 · 2016: 5 · 2015: 2
- FWCI
- 1.37
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Locations
- Biochemistry (publishedVersion, other-oa)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute of Diabetes and Digestive and Kidney Diseases (R01DK047936, R01DK066483)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Keywords
- lysine acetylation, mitochondrial protein acetylation, insulin sensitivity, skeletal muscle, ADP/ATP exchange, oxidative phosphorylation, insulin resistance, obesity, physical activity, molecular dynamics simulation, ensemble docking, mitochondrial function
- MeSH terms
- Acetylation, Adenosine Diphosphate, Adult, Binding Sites, Female, Humans, Insulin Resistance, Lysine, Male, Middle Aged, Mitochondria, Muscle, Motor Activity, Muscle Proteins, Obesity, Oxidative Phosphorylation, Protein Processing, Post-Translational, Down-Regulation, Body Mass Index, Muscle, Skeletal, Adenine Nucleotide Translocator 1, Molecular Dynamics Simulation, Molecular Docking Simulation
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