Parkin suppresses dopaminergic neuron-selective neurotoxicity induced by Pael-R in Drosophila

Neuron. 2003 Mar 27;37(6):911-24. doi: 10.1016/s0896-6273(03)00143-0.

Abstract

Parkin, an E3 ubiquitin ligase that degrades proteins with aberrant conformations, is associated with autosomal recessive juvenile Parkinsonism (AR-JP). The molecular basis of selective neuronal death in AR-JP is unknown. Here we show in an organismal system that panneuronal expression of Parkin substrate Pael-R causes age-dependent selective degeneration of Drosophila dopaminergic (DA) neurons. Coexpression of Parkin degrades Pael-R and suppresses its toxicity, whereas interfering with endogenous Drosophila Parkin function promotes Pael-R accumulation and augments its toxicity. Furthermore, overexpression of Parkin can mitigate alpha-Synuclein-induced neuritic pathology and suppress its toxicity. Our study implicates Parkin as a central player in the molecular pathway of Parkinson's disease (PD) and suggests that manipulating Parkin expression may provide a novel avenue of PD therapy.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aging
  • Animals
  • Animals, Genetically Modified
  • Blotting, Western
  • Brain / metabolism
  • Cell Death
  • Cells, Cultured
  • Dopamine / physiology*
  • Drosophila Proteins / genetics
  • Drosophila Proteins / metabolism
  • Drosophila Proteins / toxicity*
  • Drosophila*
  • Gene Expression
  • Immunohistochemistry
  • Ligases / genetics
  • Ligases / physiology*
  • Nerve Tissue Proteins / toxicity
  • Neurons / physiology*
  • Parkinson Disease
  • RNA Interference
  • Receptors, Endothelin
  • Reverse Transcriptase Polymerase Chain Reaction
  • Synucleins
  • Ubiquitin-Protein Ligases*
  • alpha-Synuclein

Substances

  • Drosophila Proteins
  • Nerve Tissue Proteins
  • Pael-R protein, Drosophila
  • Receptors, Endothelin
  • Synucleins
  • alpha-Synuclein
  • Ubiquitin-Protein Ligases
  • parkin protein
  • Ligases
  • Dopamine