The growing landscape of lysine acetylation links metabolism and cell signalling
Abstract
Lysine acetylation is a conserved protein post-translational modification that links acetyl-coenzyme A metabolism and cellular signalling. Recent advances in the identification and quantification of lysine acetylation by mass spectrometry have increased our understanding of lysine acetylation, implicating it in many biological processes through the regulation of protein interactions, activity and localization. In addition, proteins are frequently modified by other types of acylations, such as formylation, butyrylation, propionylation, succinylation, malonylation, myristoylation, glutarylation and crotonylation. The intricate link between lysine acylation and cellular metabolism has been clarified by the occurrence of several such metabolite-sensitive acylations and their selective removal by sirtuin deacylases. These emerging findings point to new functions for different lysine acylations and deacylating enzymes and also highlight the mechanisms by which acetylation regulates various cellular processes.
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Some sirtuin family members mediate non-acetyl lysine acylations, such as succinylation, malonylation and fatty acid acylation, whose cellular functions are poorly understood.
“Additionally, some members of the sirtuin family mediate non-acetyl lysine acylations (for example, succinylation, malonylation and fatty acid acylation)13–15, the cellular functions of which are so far poorly understood16.”
From NAD+ metabolism and its roles in cellular processes during ageing (2021) · cites this paper as [16]
Protein acetylation in other cellular compartments can be either inhibitory or activating.
“This stands in contrast to protein acetylation in other cellular compartments which can be either inhibitory or activating ((Choudhary et al. 2014)).”
From The Mitochondrial Acylome Emerges: Proteomics, Regulation by Sirtuins, and Metabolic and Disease Implications (2018) · cites this paper as Choudhary et al. 2014
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“It has been thought that lysine acetylation controls protein– protein interactions that regulate protein activity via acetyl-lysine-binding domains (Choudhary et al., 2014; Mujtaba et al., 2007).”
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- Authors
- Choudhary, C., Weinert, B. T., Nishida, Y., Verdin, E., & Mann, M.
- Affiliations
- University of Copenhagen (DK)
- Gladstone Institutes (US)
- Corresponding author
- Choudhary, Chunaram
- Verdin, Eric
- Mann, Matthias
- Venue
- Nature Reviews Molecular Cell Biology
- Published
- 2014-07-23
- Volume
- 15
- Issue
- 8
- Pages
- 536-550
- ISSN
- 1471-0072 (ISSN-L)
- 1471-0080
- OpenAlex
- W2064437293
- Cited by
- 1,324
- References
- 170
- Citations by year
- 2026: 76 · 2025: 82 · 2024: 89 · 2023: 94 · 2022: 111 · 2021: 113 · 2020: 118 · 2019: 114 · 2018: 146 · 2017: 131 · 2016: 134 · 2015: 99 · 2014: 16
- FWCI
- 10.97
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Reviews Molecular Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- Research at the University of Copenhagen (University of Copenhagen) (publishedVersion)
- Max Planck Digital Library (submittedVersion)
- MPG.PuRe (Max Planck Society) (submittedVersion)
- Funders
- Novo Nordisk Fonden (NNF14OC0008541)
- Topics
- Health Sciences › Medicine › Geriatrics and Gerontology › Sirtuins and Resveratrol in Medicine
- Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Histone Deacetylase Inhibitors Research
- Keywords
- lysine acetylation, post-translational modification, cellular metabolism, signal transduction, acetyl-CoA, protein acylation, protein-protein interaction, protein localization, protein function regulation
- MeSH terms
- Acetyl Coenzyme A, Acetylation, Acetyltransferases, Animals, Cells, Humans, Lysine, Protein Processing, Post-Translational, Signal Transduction, Sirtuins
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