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Regulation of Human PINK1 ubiquitin kinase by Serine167, Serine228 and Cysteine412 phosphorylation

2023-04-01

Abstract excerpt

Loss-of-function mutations in the human PINK1 kinase ( h PINK1) are causative of early-onset Parkinson’s disease (PD). Activation of h PINK1 induces phosphorylated ubiquitin to initiate removal of damaged mitochondria by autophagy. Previously we solved the structure of the insect PINK1 orthologue, Tribolium castaneum PINK1, and showed that autophosphorylation of Ser205 was critical for ubiquitin interaction and...

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Literature Corpus work
e360b064-2518-5daf-8358-2dc8505abc69
DOI
10.1101/2023.03.31.534916
Open publication

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Regulation of Human PINK1 ubiquitin kinase by Serine167, Serine228 and Cysteine412 phosphorylationDOI 10.1101/2023.03.31.534916
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