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PINK1 autophosphorylation upon membrane potential dissipation is essential for Parkin recruitment to damaged mitochondria
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Phosphorylation of parkin by Parkinson disease-linked kinase PINK1 activates parkin E3 ligase function and NF-κB signaling
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Mitofusin 1 and mitofusin 2 are ubiquitinated in a PINK1/parkin-dependent manner upon induction of mitophagy
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PINK1 stabilized by mitochondrial depolarization recruits Parkin to damaged mitochondria and activates latent Parkin for mitophagy
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Drosophila Parkin requires PINK1 for mitochondrial translocation and ubiquitinates Mitofusin
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PINK1 controls mitochondrial localization of Parkin through direct phosphorylation
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BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS (2008)
Rhomboid-7 and HtrA2/Omi act in a common pathway with the Parkinson's disease factors Pink1 and Parkin
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Parkin is recruited selectively to impaired mitochondria and promotes their autophagy
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JOURNAL OF CELL BIOLOGY (2008)
Cytoplasmic localization and proteasomal degradation of N-terminally cleaved form of PINK1
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NEUROSCIENCE LETTERS (2008)
The kinase domain of mitochondrial PINK1 faces the cytoplasm
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PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2008)
C-terminal truncation and Parkinson's disease-associated mutations down-regulate the protein serine/threonine kinase activity of PTEN-induced kinase-1
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HUMAN MOLECULAR GENETICS (2006)
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Mitochondrial pathology and muscle and dopaminergic neuron degeneration caused inactivation of Drosophila Pink1 is rescued by by Parkin
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PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2006)
Drosophila pink1 is required for mitochondrial function and interacts genetically with parkin
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Mitochondrial dysfunction in Drosophila PINK1 mutants is complemented by parkin
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Diverse effects of pathogenic mutations of parkin that catalyze multiple monoubiquitylation in vitro
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Mitochondrial import and enzymatic activity of PINK1 mutants associated to recessive parkinsonism
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HUMAN MOLECULAR GENETICS (2005)
Clinicogenetic study of PINK1 mutations in autosomal recessive early-onset parkinsonism
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Parkin phosphorylation and modulation of its E3 ubiquitin ligase activity
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Parkin functions as an E2-dependent ubiquitin-protein ligase and promotes the degradation of the synaptic vesicle-associated protein, CDCrel-1
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PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2000)
Parkin suppresses unfolded protein stress-induced cell death through its E3 ubiquitin-protein ligase activity
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JOURNAL OF BIOLOGICAL CHEMISTRY (2000)
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