Parkin is activated by PINK1-dependent phosphorylation of ubiquitin at Ser65

We have previously reported that the Parkinson's disease-associated kinase PINK1 (PTEN-induced putative kinase 1) is activated by mitochondrial depolarization and stimulates the Parkin E3 ligase by phosphorylating Ser65 within its Ubl (ubiquitin-like) domain. Using phosphoproteomic analysis, we...

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Bibliographic Details

Published in:	Biochemical journal Vol. 460; no. 1; p. 127
Main Authors:	Kazlauskaite, Agne, Kondapalli, Chandana, Gourlay, Robert, Campbell, David G, Ritorto, Maria Stella, Hofmann, Kay, Alessi, Dario R, Knebel, Axel, Trost, Matthias, Muqit, Miratul M K
Format:	Journal Article
Language:	English
Published:	England 15.05.2014
Subjects:	Amino Acid Sequence HEK293 Cells Humans Molecular Sequence Data Phosphorylation - genetics Protein Kinases - genetics Protein Kinases - physiology Serine - genetics Serine - metabolism Ubiquitin - genetics Ubiquitin - metabolism Ubiquitin-Protein Ligases - genetics Ubiquitin-Protein Ligases - metabolism
ISSN:	1470-8728, 1470-8728
Online Access:	Get more information
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