Protein lipoylation: an evolutionarily conserved metabolic regulator of health and disease. Author Elizabeth Rowland, Caroline Snowden, Ileana Cristea Publication Year 2018 Type Journal Article Abstract Lipoylation is a rare, but highly conserved lysine posttranslational modification. To date, it is known to occur on only four multimeric metabolic enzymes in mammals, yet these proteins are staples in the core metabolic landscape. The dysregulation of these mitochondrial proteins is linked to a range of human metabolic disorders. Perhaps most striking is that lipoylation itself, the proteins that add or remove the modification, as well as the proteins it decorates are all evolutionarily conserved from bacteria to humans, highlighting the importance of this essential cofactor. Here, we discuss the biological significance of protein lipoylation, the importance of understanding its regulation in health and disease states, and the advances in mass spectrometry-based proteomic technologies that can aid these studies. Keywords Bacterial Proteins, Humans, Bacteria, Mass Spectrometry, Protein Processing, Post-Translational, Proteomics, Proteins, Lysine, Metabolic Diseases, Lipoylation, Mitochondrial Proteins Journal Curr Opin Chem Biol Volume 42 Pages 76-85 Date Published 2018 Feb ISSN Number 1879-0402 DOI 10.1016/j.cbpa.2017.11.003 Alternate Journal Curr Opin Chem Biol PMCID PMC5965299 PMID 29169048 PubMedPubMed CentralGoogle ScholarBibTeXEndNote X3 XML