Functions and mechanisms of non-histone protein acetylation
Open accessAbstract
Nε-lysine acetylation was discovered more than half a century ago as a post-translational modification of histones and has been extensively studied in the context of transcription regulation. In the past decade, proteomic analyses have revealed that non-histone proteins are frequently acetylated and constitute a major portion of the acetylome in mammalian cells. Indeed, non-histone protein acetylation is involved in key cellular processes relevant to physiology and disease, such as gene transcription, DNA damage repair, cell division, signal transduction, protein folding, autophagy and metabolism. Acetylation affects protein functions through diverse mechanisms, including by regulating protein stability, enzymatic activity, subcellular localization and crosstalk with other post-translational modifications and by controlling protein-protein and protein-DNA interactions. In this Review, we discuss recent progress in our understanding of the scope, functional diversity and mechanisms of non-histone protein acetylation.
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Approved KDAC inhibitors are largely non-selective because there are only about 18 known acetyltransferases and 18 known deacetylases for thousands of acetylation sites.
“The approved KDAC inhibitors are largely non-selective, as there are only ~18 known acetyltransferases and ~18 known deacetylases for thousands of acetylation sites [25–27].”
From Acetylation: a new target for protein degradation in cancer (2025) · cites this paper as [25]
The Lysine deacetylases section says the human genome encodes 18 KDACs, and the Introduction reports thousands of acetylation sites. But the Lysine acetyltransferases section says the number of bona fide KATs is unclear and identifies 13 well-characterized KATs, not approximately 18. The Therapeutic targeting of acetylation section lists approved KDAC inhibitors but does not say they are largely non-selective or attribute their selectivity to the number of enzymes and sites. Page numbers are unavailable in our copy. (LLM, conf=0.85)
Experimental — accuracy not yet measuredChromatin modification factors including KATs GCN5, HAT1, and RTT109, and KDACs SET3, HAD1, RPD31, and HST3 are implicated in virulence processes of Candida species, including filamentous growth and biofilm formation, as well as in their resistance and sensitivity to antifungal drugs.
“Chromatin modification factors, including KATs such as GCN5, HAT1, and RTT109, as well as KDACs like SET3, HAD1, RPD31, and HST3, are implicated in the virulence processes of Candida species, including filamentous growth and biofilm formation, as well as in their resistance and sensitivity to antifungal drugs (14–16).”
From Potential role of lysine acetylation in the stepwise adaptation of <i>Candida albicans</i> to fluconazole (2025) · cites this paper as [16]
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ESCO1/2's roles in chromosome structure and interphase chromatin organizationPreprint
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“…including KATs such as GCN5 , HAT1 , and RTT109 , as well as KDACs like SET3 , HAD1, RPD31, and HST3 , are implicated in the virulence processes of Candida species, including filamentous growth and biofilm formation, as well as in their resistance and sensitivity to antifun gal drugs (14–16).”
- Authors
- Narita, T., Weinert, B. T., & Choudhary, C.
- Affiliations
- University of Copenhagen (DK)
- Corresponding author
- Choudhary, Chunaram
- Venue
- Nature Reviews Molecular Cell Biology
- Published
- 2018-11-22
- Volume
- 20
- Issue
- 3
- Pages
- 156-174
- ISSN
- 1471-0072 (ISSN-L)
- 1471-0080
- OpenAlex
- W2901164269
- Cited by
- 1,232
- References
- 184
- Citations by year
- 2026: 138 · 2025: 212 · 2024: 198 · 2023: 190 · 2022: 194 · 2021: 151 · 2020: 104 · 2019: 43 · 2018: 1
- FWCI
- 7.38
- Type
- journal article
- Language
- en
- Update notices
- correction (2019-07-02)
- Open access
- Licence
- other-oa
- www.springer.com/tdm (tdm)
- Locations
- Nature Reviews Molecular Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- Research at the University of Copenhagen (University of Copenhagen) (publishedVersion, other-oa)
- Funders
- Novo Nordisk Fonden (NNF14OC0008541)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cancer-related gene regulation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Keywords
- non-histone protein acetylation, post-translational modification, acetylome, protein stability, protein-protein interaction, protein-DNA interactions, subcellular localization, transcriptional regulation, DNA repair, signal transduction, protein folding, autophagy, metabolism
- MeSH terms
- Acetylation, Animals, Chromosomal Proteins, Non-Histone, Histones, Humans, Lysine, Protein Processing, Post-Translational, Signal Transduction, Proteome, Proteomics
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