title: The PARK2/Parkin receptor on damaged mitochondria revisited-uncovering the role of phosphorylated ubiquitin chains.
abstract: Phosphorylated ubiquitin produced by PINK1 kinase functions as a PARK2/Parkin activator by derepressing intramolecular autoinhibition of PARK2 E3 activity. Unexpectedly, we revealed that phosphorylated polyubiquitin chain also functions in the PARK2 recruitment process as a PARK2 receptor. Phosphorylated ubiquitin enables us to comprehensively understand how PINK1 and PARK2 catalyzes (phospho-)ubiquitination of depolarized mitochondria and subsequent mitophagy.
authors.affiliation: a Ubiquitin Project; Tokyo Metropolitan Institute of Medical Science ; Setagaya-ku , Tokyo.|b JST; PRESTO ; Kawaguchi , Saitama , Japan.
authors.forename: Noriyuki
authors.initials: N
authors.lastname: Matsuda
authors.affiliation: c Laboratory of Protein Metabolism; Tokyo Metropolitan Institute of Medical Science ; Setagaya-ku , Tokyo , Japan.
authors.forename: Keiji
authors.initials: K
authors.lastname: Tanaka
mesh_terms: D008928:Mitochondria / Q000378:metabolism*; D063306:Mitophagy; D008954:Models, Biological; D010766:Phosphorylation; D025801:Ubiquitin / Q000378:metabolism*; D044767:Ubiquitin-Protein Ligases / Q000378:metabolism*
chemical_list: D025801:Ubiquitin; D044767:Ubiquitin-Protein Ligases; C111567:parkin protein
keywords: PARK2 receptor; PARK2/Parkin; PINK1; mitochondria; phosphorylated ubiquitin