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Article
Biochemistry & Molecular Biology
Structural basis for feedforward control in the PINK1/Parkin pathway
Veronique Sauve et al.
Summary: PINK1 and parkin play a crucial role in mitochondrial quality control and are often mutated in Parkinson's disease. PINK1 phosphorylates ubiquitin and the Ubl domain of parkin to regulate the localization and activity of parkin. The study discovered that phospho-ubiquitin can bind to two different sites on parkin, controlling its localization and releasing its autoinhibition. Activation of parkin by phosphorylated ubiquitin plays a significant role in the PINK1-parkin pathway.
EMBO JOURNAL (2022)
Article
Biochemistry & Molecular Biology
Structure of the second phosphoubiquitin-binding site in parkin
Rayan Fakih et al.
Summary: Parkin and PINK1 regulate a mitochondrial quality control system that is mutated in some early onset forms of Parkinson's disease. Recently, an alternative feed-forward mechanism was identified that bypasses the need for parkin phosphorylation. This study reveals the structure of parkin activated through this feed-forward mechanism and provides insights into the differences in specificity and affinity of the binding sites.
JOURNAL OF BIOLOGICAL CHEMISTRY (2022)
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