Cited by 1,324Sirtuins and Resveratrol in MedicineAdvanced Proteomics Techniques and ApplicationsHistone Deacetylase Inhibitors Research

The growing landscape of lysine acetylation links metabolism and cell signalling

Choudhary, Chunaram, Weinert, Brian T., Nishida, Yuya, Verdin, Eric, Mann, Matthias·2014·Nature Reviews Molecular Cell Biology

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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Crossref · 10.1038/nrm3841

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170 of 170 references verified0 citation errors · 0 not checkable

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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.”
  • 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)).”

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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
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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