Protein lipoylation: an evolutionarily conserved metabolic regulator of health and disease
| Autor: | Caroline K. Snowden, Elizabeth A. Rowland, Ileana M. Cristea |
|---|---|
| Rok vydání: | 2018 |
| Předmět: |
Proteomics
0301 basic medicine Lipoylation Lysine Microbial metabolism Regulator Biology Biochemistry Mass Spectrometry Article Cofactor Analytical Chemistry Mitochondrial Proteins 03 medical and health sciences Bacterial Proteins Metabolic Diseases Humans Genetics Bacteria Proteins biology.organism_classification 030104 developmental biology biology.protein Protein Processing Post-Translational Protein lipoylation |
| Zdroj: | Current Opinion in Chemical Biology. 42:76-85 |
| ISSN: | 1367-5931 |
| DOI: | 10.1016/j.cbpa.2017.11.003 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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