Functions and mechanisms of non-histone protein acetylation

Nat Rev Mol Cell Biol. 2019 Mar;20(3):156-174. doi: 10.1038/s41580-018-0081-3.


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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Acetylation
  • Animals
  • Chromosomal Proteins, Non-Histone / metabolism*
  • Chromosomal Proteins, Non-Histone / physiology*
  • Histones / metabolism
  • Humans
  • Lysine / metabolism
  • Protein Processing, Post-Translational
  • Proteome / metabolism
  • Proteomics
  • Signal Transduction


  • Chromosomal Proteins, Non-Histone
  • Histones
  • Proteome
  • Lysine