Disruption of protein quality control in Parkinson's disease

Cold Spring Harb Perspect Med. 2012 May;2(5):a009423. doi: 10.1101/cshperspect.a009423.

Abstract

Parkinson's disease (PD), like a number of neurodegenerative diseases associated with aging, is characterized by the abnormal accumulation of protein in a specific subset of neurons. Although researchers have recently elucidated the genetic causes of PD, much remains unknown about what causes increased protein deposition in the disease. Given that increased protein aggregation may result not only from an increase in production, but also from decreased protein clearance, it is imperative to investigate both possibilities as potential PD culprits. This article provides a review of the systems that regulate protein clearance, including the ubiquitin proteasome system (UPS) and the autophagy-lysosomal pathway. Literature implicating failure of these mechanisms-such as UPS dysfunction resulting from environmental toxins and mutations in α-synuclein and parkin, as well as macroautophagic pathway failure because of oxidative stress and aging-in the pathogenesis of PD is also discussed.

Publication types

  • Review

MeSH terms

  • Adenosine Triphosphatases / genetics
  • Aging / physiology
  • Animals
  • Autophagy / physiology*
  • Environmental Pollutants / toxicity
  • Humans
  • Lysosomes / physiology*
  • Mice
  • Mutation / genetics
  • Oxidative Stress / physiology
  • Parkinson Disease / etiology*
  • Parkinson Disease / genetics
  • Parkinson Disease / metabolism
  • Proteasome Endopeptidase Complex / physiology*
  • Protein Folding / drug effects
  • Proteins / metabolism*
  • Proteolysis
  • Proteostasis Deficiencies / etiology*
  • Proteostasis Deficiencies / genetics
  • Proteostasis Deficiencies / metabolism
  • Rats
  • Risk Factors
  • Signal Transduction / physiology
  • Ubiquitin / physiology*

Substances

  • Environmental Pollutants
  • Proteins
  • Ubiquitin
  • Proteasome Endopeptidase Complex
  • Adenosine Triphosphatases