Regulation of cellular metabolism by protein lysine acetylation
Open accessAbstract
Metabolic Regulation Through Acetylation: Covalent modification of lysine residues in various proteins in the nucleus is a recognized mechanism for control of transcription. Now two papers suggest that acetylation may represent an important regulatory mechanism controlling the function of metabolic enzymes (see the Perspective by Norvell and McMahon ). Zhao et al. (p. 1000 ) found that a large proportion of enzymes in various metabolic pathways were acetylated in human liver cells. Acetylation regulated various enzymes by distinct mechanisms, directly activating some, inhibiting one, and controlling the stability of another. Control of metabolism by acetylation appears to be evolutionarily conserved: Wang et al. (p. 1004 ) found that the ability of the bacterium Salmonella entericum to optimize growth on distinct carbon sources required differential acetylation of key metabolic enzymes, thus controlling flux through metabolic pathways.
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There is a profound overlap between acetylated proteins in the cytosol and proteins involved in metabolic processes.
“This theory is further evidenced by a profound overlap between acetylated proteins in the cytosol and proteins involved in metabolic processes [10–13,53,54].”
From Acetylation: a new target for protein degradation in cancer (2025) · cites this paper as [54]
Acetylation of mitochondrial proteins is a pivotal post-transcriptional modification governing mitochondrial metabolism.
“Acetylation of mitochondrial proteins has been described as a pivotal post-transcriptional modification in governing mitochondrial metabolism as shown by the acetylation of the intermediate metabolic enzymes involved in the tricarboxylic acid cycle and fatty acid β-oxidation (Zhao et al., 2010).”
From Mitochondrial (Dys)function and Insulin Resistance: From Pathophysiological Molecular Mechanisms to the Impact of Diet (2019) · cites this paper as Zhao et al., 2010
Acetyl-CoA can influence metabolic flux through acetylation of metabolic enzymes, reinforcing pathways such as glycolysis when carbon availability is high.
“Acetyl-CoA can also influence metabolic flux through acetylation of metabolic enzymes (49, 50), reinforcing metabolic pathways such as glycolysis when carbon availability is high.”
From Fueling Immunity: Insights into Metabolism and Lymphocyte Function (2013) · cites this paper as [50]
Many cellular proteins besides histones are acetylated, including most enzymes in core metabolic pathways.
“Many other cellular proteins besides histones are acetylated, including most of the enzymes in core metabolic pathways (Zhao et al., 2010).”
From Cellular Metabolism and Disease: What Do Metabolic Outliers Teach Us? (2012) · cites this paper as Zhao et al., 2010
In both mammals and bacteria, enzyme acetylation fluctuates according to which nutrients are available to the cell.
“In both mammals and bacteria, enzyme acetylation fluctuates according to which nutrients are available to the cell (Wang et al., 2010; Zhao et al., 2010).”
From Cellular Metabolism and Disease: What Do Metabolic Outliers Teach Us? (2012) · cites this paper as Zhao et al., 2010
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- Authors
- Zhao, S., Xu, W., Jiang, W., Yu, W., Lin, Y., Zhang, T., Yao, J., Zhou, L., Zeng, Y., Li, H., Li, Y., Shi, J., An, W., Hancock, S. M., He, F., Qin, L., Chin, J., Yang, P., Chen, X., Lei, Q., Xiong, Y., & Guan, K.-L.
- Affiliations
- Fudan University (CN)
- University of North Carolina at Chapel Hill (US)
- Chinese Academy of Sciences (CN)
- MRC Laboratory of Molecular Biology (GB)
- Affiliated Zhongshan Hospital, Fudan University, Shanghai 20032, China.
- School of Life Sciences, Fudan University, Shanghai 20032, China.
- Corresponding author
- Xu, Wei
- Jiang, Wenqing
- Xiong, Yue
- Guan, Kun-Liang
- ORCID
- Venue
- Science
- Published
- 2010-02-19
- Volume
- 327
- Issue
- 5968
- Pages
- 1000-1004
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- PMC
- PMC3232675
- OpenAlex
- W2087714970
- Cited by
- 1,910
- References
- 15
- Citations by year
- 2026: 60 · 2025: 82 · 2024: 88 · 2023: 95 · 2022: 106 · 2021: 124 · 2020: 98 · 2019: 129 · 2018: 103 · 2017: 131 · 2016: 150 · 2015: 136 · 2014: 143 · 2013: 137 · 2012: 160
- FWCI
- 71.92
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Carolina Digital Repository (University of North Carolina at Chapel Hill) (submittedVersion)
- UNC Libraries
- Funders
- National Natural Science Foundation of China
- National Institutes of Health
- National Cancer Institute (R01CA065572, R01CA65572, R01CA108941)
- National Institute of General Medical Sciences (R01GM51586, R01GM051586)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Biochemical Acid Research Studies
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cancer-related gene regulation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Keywords
- lysine acetylation, post-translational modification, metabolic regulation, metabolic enzymes, human liver, glycolysis, gluconeogenesis, TCA cycle, urea cycle, fatty acid oxidation, glycogen metabolism, enoyl-CoA hydratase, malate dehydrogenase, argininosuccinate lyase, phosphoenolpyruvate carboxykinase
- MeSH terms
- Acetylation, Argininosuccinate Lyase, Cell Line, Citric Acid Cycle, Enoyl-CoA Hydratase, Enzymes, Fatty Acids, Gluconeogenesis, Glycogen, Glycolysis, Humans, Isomerases, Liver, Lysine, Malate Dehydrogenase, Multienzyme Complexes, Oxidation-Reduction, Phosphoenolpyruvate Carboxykinase (GTP), Protein Processing, Post-Translational, Proteins, Urea, 3-Hydroxyacyl CoA Dehydrogenases, Proteome, Hepatocytes, Intracellular Signaling Peptides and Proteins, Peroxisomal Bifunctional Enzyme
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