MPP+ impairs autophagic clearance of alpha-synuclein by impairing the activity of dynein

Neuroreport. 2009 Apr 22;20(6):569-73. doi: 10.1097/WNR.0b013e32832986c4.

Abstract

Increasing evidence suggests that dynein has an important role in the clearance of misfolded proteins by autophagy. Here we show that treatment of cells with 1-methyl-4-phenylpyridinium (MPP) cause alpha-synuclein overexpression and aggregation, leading to the accumulation of autophagic vacuoles and the recruitment of LC3-II to these vacuoles in the cytoplasm. After MPP treatment, dynein expression decreased and was mainly aggregated at the periphery of cytoplasm and lost its colocalization with alpha-synuclein and lamp1, indicating that dynein lost its function in the aggresome formation and failed to return autophagosome and lysosomes to the center of the cell for degradation. We consider that dynein plays an important role in the autophagic clearance of aggregate-prone proteins.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • 1-Methyl-4-phenylpyridinium / pharmacology*
  • Animals
  • Autophagy / drug effects
  • Autophagy / physiology*
  • Catalase / metabolism
  • Cytoplasm / metabolism
  • Dyneins / metabolism*
  • Enzyme Inhibitors / pharmacology
  • Lysosomal Membrane Proteins / metabolism
  • Lysosomes / metabolism
  • Microtubule-Associated Proteins / metabolism
  • Neurons / drug effects
  • Neurons / physiology*
  • PC12 Cells
  • RNA, Messenger / metabolism
  • Rats
  • Staurosporine / pharmacology
  • Superoxide Dismutase / metabolism
  • alpha-Synuclein / metabolism*

Substances

  • Enzyme Inhibitors
  • LC3 protein, rat
  • Lamp1 protein, rat
  • Lysosomal Membrane Proteins
  • Microtubule-Associated Proteins
  • RNA, Messenger
  • alpha-Synuclein
  • Catalase
  • Superoxide Dismutase
  • Dyneins
  • Staurosporine
  • 1-Methyl-4-phenylpyridinium