The Chemical Biology of Reversible Lysine Post-translational Modifications

Cell Chem Biol. 2020 Aug 20;27(8):953-969. doi: 10.1016/j.chembiol.2020.07.002. Epub 2020 Jul 21.

Abstract

Lysine (Lys) residues in proteins undergo a wide range of reversible post-translational modifications (PTMs), which can regulate enzyme activities, chromatin structure, protein-protein interactions, protein stability, and cellular localization. Here we discuss the "writers," "erasers," and "readers" of some of the common protein Lys PTMs and summarize examples of their major biological impacts. We also review chemical biology approaches, from small-molecule probes to protein chemistry technologies, that have helped to delineate Lys PTM functions and show promise for a diverse set of biomedical applications.

Keywords: acetylation; acetyltransferase; bromodomain; deacetylase; enzyme; methylation; ubiquitination.

Publication types

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

MeSH terms

  • Acetylation
  • Lysine / metabolism*
  • Lysine Acetyltransferases / metabolism
  • Methylation
  • Protein Methyltransferases / metabolism
  • Small Molecule Libraries / chemistry
  • Small Molecule Libraries / metabolism
  • Ubiquitin-Specific Proteases / metabolism
  • Ubiquitination

Substances

  • Small Molecule Libraries
  • Protein Methyltransferases
  • Lysine Acetyltransferases
  • Ubiquitin-Specific Proteases
  • Lysine