Lysine Acetylation Targets Protein Complexes and Co-Regulates Major Cellular Functions

TLDR

Lysine acetylation is a covalent post‑translational modification that regulates protein activity. The study aimed to assess the prevalence of lysine acetylation across the entire proteome. Mass spectrometry advances enabled the authors to survey lysine acetylation proteome‑wide. Acetylation is far more widespread than previously appreciated, affecting proteins involved in diverse biological functions, modulating phosphorylation susceptibility, occurring on enzymes that regulate ubiquitination and on components of large macromolecular complexes, and providing insight into the mechanisms of lysine deacetylase inhibitors that show clinical promise for cancer treatment.

Abstract

Lysine Acetylation Catalog Covalent posttranslational modification is an essential cellular regulatory mechanism by which the activity of proteins can be controlled. Advances in mass spectrometry made it possible for Choudhary et al. (p. 834 , published online 16 July) to assess the prevalence of lysine acetylation throughout the whole proteome. Acetylation is much more widespread than previously appreciated and occurs on proteins participating in all sorts of biological functions. Acetylation can influence susceptibility of proteins to phosphorylation and occurs frequently on enzymes that control the modification of other proteins by covalent ubiquitination and on proteins that form large macromolecular complexes. The findings also help to characterize the actions of lysine deacetylase inhibitors, which have shown clinical promise in treatments for cancer.