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

J Neurosci. 2007 Nov 7;27(45):12413-8. doi: 10.1523/JNEUROSCI.0719-07.2007.

Abstract

Degeneration of dopaminergic neurons in the substantia nigra is characteristic for Parkinson's disease (PD), the second most common neurodegenerative disorder. Mitochondrial dysfunction is believed to contribute to the etiology of PD. Although most cases are sporadic, recent evidence points to a number of genes involved in familial variants of PD. Among them, a loss-of-function of phosphatase and tensin homolog-induced kinase 1 (PINK1; PARK6) is associated with rare cases of autosomal recessive parkinsonism. In HeLa cells, RNA interference-mediated downregulation of PINK1 results in abnormal mitochondrial morphology and altered membrane potential. Morphological changes of mitochondria can be rescued by expression of wild-type PINK1 but not by PD-associated PINK1 mutants. Moreover, primary cells derived from patients with two different PINK1 mutants showed a similar defect in mitochondrial morphology. Human parkin but not PD-associated mutants could rescue mitochondrial pathology in human cells like wild-type PINK1. Our results may therefore suggest that PINK1 deficiency in humans results in mitochondrial abnormalities associated with cellular stress, a pathological phenotype, which can be ameliorated by enhanced expression of parkin.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cells, Cultured
  • HeLa Cells
  • Humans
  • Mitochondria / enzymology*
  • Mitochondria / genetics
  • Mitochondria / pathology*
  • Mitochondrial Membranes / enzymology
  • Mitochondrial Membranes / metabolism
  • Mitochondrial Membranes / pathology
  • Parkinson Disease / genetics
  • Parkinson Disease / metabolism
  • Parkinson Disease / pathology
  • Parkinsonian Disorders / genetics
  • Parkinsonian Disorders / metabolism
  • Parkinsonian Disorders / pathology
  • Phenotype
  • Protein Kinases / deficiency
  • Protein Kinases / genetics
  • Protein Kinases / physiology*
  • Ubiquitin-Protein Ligases / physiology*

Substances

  • Ubiquitin-Protein Ligases
  • parkin protein
  • Protein Kinases
  • PTEN-induced putative kinase