PINK1 is recruited to mitochondria with parkin and associates with LC3 in mitophagy (Q24299149)

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Shinji Saiki

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Shigeto Sato

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Fumiaki Sato

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Taku Hatano

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Hiroto Eguchi

Expanding insights of mitochondrial dysfunction in Parkinson's disease.

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language of work or name

English

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publication date

19 March 2010

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published in

FEBS Letters

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volume

584

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issue

6

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page(s)

1073-9

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cites work

1 reference

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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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Pink1 regulates mitochondrial dynamics through interaction with the fission/fusion machinery

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Fission and selective fusion govern mitochondrial segregation and elimination by autophagy

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Parkin is recruited selectively to impaired mitochondria and promotes their autophagy

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PINK1 controls mitochondrial localization of Parkin through direct phosphorylation

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PINK1-dependent recruitment of Parkin to mitochondria in mitophagy

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LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing

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Leucine-rich repeat kinase 2 associates with lipid rafts

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Loss of PINK1 function promotes mitophagy through effects on oxidative stress and mitochondrial fission

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Mitochondrial import and enzymatic activity of PINK1 mutants associated to recessive parkinsonism

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Mutations in PTEN-induced putative kinase 1 associated with recessive parkinsonism have differential effects on protein stability

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Molecular interaction between parkin and PINK1 in mammalian neuronal cells

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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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Loss-of-function of human PINK1 results in mitochondrial pathology and can be rescued by parkin

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Wild-type PINK1 prevents basal and induced neuronal apoptosis, a protective effect abrogated by Parkinson disease-related mutations

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PINK1 protects against oxidative stress by phosphorylating mitochondrial chaperone TRAP1

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