Protein lysine acetylation and its role in different human pathologies: a proteomic approach

Introduction Lysine acetylation is a reversible post-translational modification (PTM) regulated through the action of specific types of enzymes: lysine acetyltransferases (KATs) and lysine deacetylases (HDACs), in addition to bromodomains, which are a group of conserved domains which identify acetylated lysine residues, several of the players in the process of protein acetylation, including enzymes and bromodomain-containing proteins, have been related to the progression of several diseases. The combination of high-resolution mass spectrometry-based proteomics, and immunoprecipitation to enrich acetylated peptides has contributed in recent years to expand the knowledge about this PTM described initially in histones and nuclear proteins, and is currently reported in more than 5000 human proteins, that are regulated by this PTM. Areas Covered This review presents an overview of the main participant elements, the scenario in the development of protein lysine acetylation, and its role in different human pathologies. Expert opinion Acetylation targets are practically all cellular processes in eukaryotes and prokaryotes organisms. Consequently, this modification has been linked to many pathologies like cancer, viral infection, obesity, diabetes, cardiovascular, and nervous system-associated diseases, to mention a few relevant examples. Accordingly, some intermediate mediators in the acetylation process have been projected as therapeutic targets.

Automated summary

Lysine acetylation is a crucial reversible post-translational modification regulated by enzymes and bromodomain-containing proteins, with implications in the progression of various diseases. The use of mass spectrometry-based proteomics and immunoprecipitation has expanded our knowledge on this modification, now reported in over 5000 human proteins.