Beyond its role in mitochondrial bioenergetics, Coenzyme Q (CoQ, ubiquinone) serves as a key membrane-embedded antioxidant throughout the cell. However, how CoQ is moved from its site of synthesis on the inner mitochondrial membrane to other sites remains a longstanding mystery. In a recent study, researchers identified two highly conserved but poorly characterized mitochondrial proteins that affect this process. Their results reveal the protein machinery central to CoQ trafficking in yeast and lend insights into the broader interplay between mitochondria and the rest of the cell.
Read the article: UbiB proteins regulate cellular CoQ distribution in Saccharomyces cerevisiae