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Logo of jbcThe Journal of Biological Chemistry
 
J Biol Chem. 2015 October 16; 290(42): 25212.
PMCID: PMC4646172

Understanding How the Ubiquitin Ligase Parkin Interacts with a Phosphorylated Ubiquitin for Activation

Site-specific Interaction Mapping of Phosphorylated Ubiquitin to Uncover Parkin Activation

See referenced article, J. Biol. Chem. 2015, 290, 25199–25211

When mitochondria get damaged, they are removed by autophagy. One of the critical players in the autophagy pathway is a cytosolic E3 ubiquitin ligase called Parkin. In the familial form of Parkinson disease, the gene for Parkin can be mutated. Researchers know that the phosphorylation of Parkin and ubiquitin is important for the activation and recruitment of Parkin to damaged mitochondria, but the underlying mechanism is unknown. In this Paper of the Week, a team led by Koji Yamano and Noriyuki Matsuda at the Tokyo Metropolitan Institute of Medical Science described the interactions between phosphorylated Parkin and ubiquitin. They found that two domains in Parkin, the in-between-RING domain and the RING1 domain, relied on phosphorylation to bind to ubiquitin. The authors say that their analyses suggest that “a novel binding mechanism between Parkin and ubiquitin leads to a Parkin conformational change with subsequent activation of Parkin E3 ligase activity.”

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Computational modeling of activated Parkin with a phosphorylated ubiquitin.


Articles from The Journal of Biological Chemistry are provided here courtesy of American Society for Biochemistry and Molecular Biology