Posttranslational modification

Gene

Acetylation

Enzyme

Chemistry

Lysine

Epigenetics

Amino acid

Biochemistry

Histone

Computational biology

Biology

Cell biology

Chemical Reviews

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.

Lysine Acetylation Goes Global: From Epigenetics to Metabolism and Therapeutics