Ubiquitin is phosphorylated by PINK1 to activate parkin

• Published in: Nature (London) Vol. 510; no. 7503; pp. 162 - 166
• Main Authors: Koyano, Fumika, Okatsu, Kei, Kosako, Hidetaka, Tamura, Yasushi, Go, Etsu, Kimura, Mayumi, Kimura, Yoko, Tsuchiya, Hikaru, Yoshihara, Hidehito, Hirokawa, Takatsugu, Endo, Toshiya, Fon, Edward A., Trempe, Jean-François, Saeki, Yasushi, Tanaka, Keiji, Matsuda, Noriyuki
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 05.06.2014; Nature Publishing Group
• Subjects: 14; 14/19; 631/378/1689/1718; 631/45/474/2073; 631/80/304; 631/80/642/333; 82; 82/51; 82/58; Animals; Cell culture; Enzyme Activation; Fibroblasts; Genetic aspects; HeLa Cells; Humanities and Social Sciences; Humans; Kinases; letter; Membrane Potential, Mitochondrial; Mice; Mitochondria; Mitochondria - metabolism; multidisciplinary; Mutation; Mutation - genetics; Parkinson Disease; Parkinson's disease; Parkinsonism; Phosphorylation; Phosphoserine - metabolism; Phosphotransferases; Physiological aspects; Protein Kinases - metabolism; Proteins; Quality control; Science; Studies; Ubiquitin; Ubiquitin - chemistry; Ubiquitin - metabolism; Ubiquitin-Protein Ligases - genetics; Ubiquitin-Protein Ligases - metabolism; Ubiquitination

Ubiquitin, known for its role in post-translational modification of other proteins, undergoes post-translational modification itself; after a decrease in mitochondrial membrane potential, the kinase enzyme PINK1 phosphorylates ubiquitin at Ser 65, and the phosphorylated ubiquitin then interacts with...