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

Elizabeth A. Rowland, Caroline K. Snowden, Ileana M. Cristea

Research output: Contribution to journalReview articlepeer-review

12 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)76-85
Number of pages10
JournalCurrent Opinion in Chemical Biology
Volume42
DOIs
StatePublished - Feb 2018

All Science Journal Classification (ASJC) codes

  • Analytical Chemistry
  • Biochemistry

Fingerprint Dive into the research topics of 'Protein lipoylation: an evolutionarily conserved metabolic regulator of health and disease'. Together they form a unique fingerprint.

Cite this