PINK1 is activated by mitochondrial membrane potential depolarization and stimulates Parkin E3 ligase activity by phosphorylating Serine 65

Missense mutations in PTEN-induced kinase 1 (PINK1) cause autosomal-recessive inherited Parkinson's disease (PD). We have exploited our recent discovery that recombinant insect PINK1 is catalytically active to test whether PINK1 directly phosphorylates 15 proteins encoded by PD-associated genes...

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Bibliographic Details
Published in:	Open biology Vol. 2; no. 5; p. 120080
Main Authors:	Kondapalli, Chandana, Kazlauskaite, Agne, Zhang, Ning, Woodroof, Helen I., Campbell, David G., Gourlay, Robert, Burchell, Lynn, Walden, Helen, Macartney, Thomas J., Deak, Maria, Knebel, Axel, Alessi, Dario R., Muqit, Miratul M. K.
Format:	Journal Article
Language:	English
Published:	England The Royal Society 01.05.2012
Subjects:	Animals Carbonyl Cyanide m-Chlorophenyl Hydrazone - pharmacology Enzyme Activation - drug effects HEK293 Cells Humans Insect Proteins - genetics Insect Proteins - physiology Membrane Potential, Mitochondrial - physiology Parkin Parkinson Disease - metabolism Parkinson's Disease Phosphorylation - drug effects Phosphoserine - metabolism Phosphothreonine - metabolism PINK1 Protein Kinases - genetics Protein Kinases - physiology Protein Processing, Post-Translational - drug effects Protein Stability - drug effects Protein Structure, Tertiary Receptor-Like Protein Tyrosine Phosphatases, Class 2 - pharmacology Recombinant Fusion Proteins - physiology RNA Interference RNA, Small Interfering - pharmacology Tribolium - enzymology Tribolium - genetics Ubiquitin-Protein Ligases - metabolism PINK1 Parkinson's disease Parkin
ISSN:	2046-2441, 2046-2441
Online Access:	Get full text
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