Climbing the scaffolds of Parkinson's disease pathogenesis

Neuron. 2007 Feb 15;53(4):469-70. doi: 10.1016/j.neuron.2007.02.002.

Abstract

Several neurodegenerative disorders, including Parkinson's and Alzheimer's diseases, are characterized neuropathologically by accumulation of misfolded proteins such as alpha-synuclein that disrupts scaffold molecules in the caveolae. A new study by Ihara et al. in this issue of Neuron shows that a novel scaffold protein, Sept4, may be an important player in modulating the pathological alterations of alpha-synuclein in models of Parkinson's disease, suggesting that gene therapies targeting scaffold proteins might be effective in the treatment of neurodegenerative disorders.

Publication types

  • Research Support, N.I.H., Extramural
  • Comment

MeSH terms

  • Animals
  • Cytoskeletal Proteins / metabolism*
  • GTP Phosphohydrolases / metabolism*
  • Humans
  • Neurons / metabolism
  • Parkinson Disease* / etiology
  • Parkinson Disease* / metabolism
  • Parkinson Disease* / pathology
  • Protein Folding
  • Septins
  • alpha-Synuclein / metabolism

Substances

  • Cytoskeletal Proteins
  • alpha-Synuclein
  • GTP Phosphohydrolases
  • SEPTIN4 protein, human
  • Septins