Article
Binding to serine 65-phosphorylated ubiquitin primes Parkin for optimal PINK1-dependent phosphorylation and activation.
EMBO reports - 1 Aug 2015
Kazlauskaite Agne, Martínez-Torres R Julio, Wilkie Scott, Kumar Atul, Peltier Julien, Gonzalez Alba, Johnson Clare, Zhang Jinwei, Hope Anthony G, Peggie Mark, Trost Matthias, van Aalten Daan M F, Alessi Dario R, Prescott Alan R, Knebel Axel, Walden Helen, Muqit Miratul M K
Abstract excerpt
Mutations in the mitochondrial protein kinase PINK1 are associated with autosomal recessive Parkinson disease (PD). We and other groups have reported that PINK1 activates Parkin E3 ligase activity both directly via phosphorylation of Parkin serine 65 (Ser(65))--which lies within its ubiquitin-like domain (Ubl)--and indirectly through phosphorylation of ubiquitin at Ser(65). How Ser(65)-phosphorylated ubiquitin...
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