Protein lipoylation: an evolutionarily conserved metabolic regulator of health and disease.

TitleProtein lipoylation: an evolutionarily conserved metabolic regulator of health and disease.
Publication TypeJournal Article
Year of Publication2018
AuthorsRowland, EA, Snowden, CK, Cristea, IM
JournalCurr Opin Chem Biol
Volume42
Pagination76-85
Date Published2018 02
ISSN1879-0402
KeywordsBacteria, Bacterial Proteins, Humans, Lipoylation, Lysine, Mass Spectrometry, Metabolic Diseases, Mitochondrial Proteins, Protein Processing, Post-Translational, Proteins, Proteomics
Abstract

<p>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.</p>

DOI10.1016/j.cbpa.2017.11.003
Alternate JournalCurr Opin Chem Biol
PubMed ID29169048
PubMed Central IDPMC5965299
Grant ListR01 GM114141 / GM / NIGMS NIH HHS / United States
R01 HL127640 / HL / NHLBI NIH HHS / United States