Site-specific interaction mapping of phosphorylated ubiquitin to uncover Parkin activation

Abstract

Background: Phosphorylation of both Parkin and ubiquitin by PINK1 is crucial for Parkin E3 ligase activity; however, the mechanism remains unknown. Results: Site-specific photo-crosslinking identified the phosphorylation-dependent interaction surface between Parkin and ubiquitin. Conclusion: IBR along with RING1 domain of Parkin provides an interaction site for ubiquitin. Significance: A novel binding mechanism with phosphorylated ubiquitin leads to a Parkin conformational change.