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• W2566705091 abstract "Significance Parkinson’s disease is a devastating neurodegenerative disorder that can be inherited through mutations in genes encoding the kinase PTEN-induced kinase 1 (PINK1) or the ubiquitin ligase parkin. Parkin exhibits neuroprotective properties by ubiquitinating proteins on damaged mitochondria, leading to their turnover. However, parkin exists in an inactive state that must be alleviated by PINK1 phosphorylation. Therefore, the molecular interpretation of the phosphorylation signal is immensely valuable to our understanding of parkin’s role in mitochondrial maintenance and neuronal fidelity. We present the 3D structure of the phosphorylated inhibitory domain of parkin and describe the structural changes that lead to activation of the enzyme. Alongside the available phosphoubiquitin structure, this study completes a structural picture of PINK1-orchestrated parkin activation in impaired mitochondria." @default.
• W2566705091 created "2017-01-06" @default.
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• W2566705091 date "2016-12-22" @default.
• W2566705091 modified "2023-10-15" @default.
• W2566705091 title "Structure of phosphorylated UBL domain and insights into PINK1-orchestrated parkin activation" @default.
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• W2566705091 doi "https://doi.org/10.1073/pnas.1613040114" @default.
• W2566705091 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5240717" @default.
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• W2566705091 hasPublicationYear "2016" @default.
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