Lysine Acetylation Goes Global: From Epigenetics to Metabolism and Therapeutics

Chem Rev. 2018 Feb 14;118(3):1216-1252. doi: 10.1021/acs.chemrev.7b00181. Epub 2018 Feb 6.

Abstract

Post-translational acetylation of lysine residues has emerged as a key regulatory mechanism in all eukaryotic organisms. Originally discovered in 1963 as a unique modification of histones, acetylation marks are now found on thousands of nonhistone proteins located in virtually every cellular compartment. Here we summarize key findings in the field of protein acetylation over the past 20 years with a focus on recent discoveries in nuclear, cytoplasmic, and mitochondrial compartments. Collectively, these findings have elevated protein acetylation as a major post-translational modification, underscoring its physiological relevance in gene regulation, cell signaling, metabolism, and disease.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Acetylation
  • Epigenomics*
  • Histone Deacetylase Inhibitors / chemistry
  • Histone Deacetylase Inhibitors / metabolism
  • Histone Deacetylase Inhibitors / therapeutic use
  • Histone Deacetylases / chemistry
  • Histone Deacetylases / metabolism
  • Histones / metabolism*
  • Humans
  • Lysine / metabolism
  • Lysine Acetyltransferases / chemistry
  • Lysine Acetyltransferases / metabolism
  • Mitochondria / metabolism
  • Protein Stability

Substances

  • Histone Deacetylase Inhibitors
  • Histones
  • Lysine Acetyltransferases
  • Histone Deacetylases
  • Lysine