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Publication Detail
The Parkinson's disease-linked proteins Fbxo7 and Parkin interact to mediate mitophagy.
  • Publication Type:
    Journal article
  • Publication Sub Type:
    Journal Article
  • Authors:
    Burchell VS, Nelson DE, Sanchez-Martinez A, Delgado-Camprubi M, Ivatt RM, Pogson JH, Randle SJ, Wray S, Lewis PA, Houlden H, Abramov AY, Hardy J, Wood NW, Whitworth AJ, Laman H, Plun-Favreau H
  • Publication date:
    09/2013
  • Pagination:
    1257, 1265
  • Journal:
    Nat Neurosci
  • Volume:
    16
  • Issue:
    9
  • Status:
    Published
  • Country:
    United States
  • PII:
    nn.3489
  • Language:
    eng
  • Keywords:
    Animals, Animals, Genetically Modified, Carbonyl Cyanide m-Chlorophenyl Hydrazone, Cell Line, Tumor, Cells, Cultured, Drosophila, F-Box Proteins, Female, Fertility, Fibroblasts, Humans, Male, Microtubule-Associated Proteins, Mitochondria, Mitochondrial Degradation, Mutation, Parkinson Disease, Protein Transport, Proton Ionophores, RNA, Small Interfering, Time Factors, Ubiquitin-Protein Ligases, Ubiquitination
Abstract
Compelling evidence indicates that two autosomal recessive Parkinson's disease genes, PINK1 (PARK6) and Parkin (PARK2), cooperate to mediate the autophagic clearance of damaged mitochondria (mitophagy). Mutations in the F-box domain-containing protein Fbxo7 (encoded by PARK15) also cause early-onset autosomal recessive Parkinson's disease, by an unknown mechanism. Here we show that Fbxo7 participates in mitochondrial maintenance through direct interaction with PINK1 and Parkin and acts in Parkin-mediated mitophagy. Cells with reduced Fbxo7 expression showed deficiencies in translocation of Parkin to mitochondria, ubiquitination of mitofusin 1 and mitophagy. In Drosophila, ectopic overexpression of Fbxo7 rescued loss of Parkin, supporting a functional relationship between the two proteins. Parkinson's disease-causing mutations in Fbxo7 interfered with this process, emphasizing the importance of mitochondrial dysfunction in Parkinson's disease pathogenesis.
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Clinical and Movement Neurosciences
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Neurodegenerative Diseases
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Department of Neuromuscular Diseases
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Neurodegenerative Diseases
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Clinical and Movement Neurosciences
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Neurodegenerative Diseases
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