Chaperone proteostasis in Parkinson's disease: stabilization of the Hsp70/alpha-synuclein complex by Hip.

@article{Roodveldt2009ChaperonePI,
  title={Chaperone proteostasis in Parkinson's disease: stabilization of the Hsp70/alpha-synuclein complex by Hip.},
  author={Cintia Roodveldt and Carlos W. Bertoncini and August Andersson and Annemieke T van der Goot and Shang-Te Danny Hsu and Rafael Fern{\'a}ndez-Montesinos and Jannie de Jong and Tjakko J. van Ham and Ellen A. A. Nollen and David Patricio Viscarra del Pozo and John C. Christodoulou and Christopher M. Dobson},
  journal={The EMBO journal},
  year={2009},
  volume={28 23},
  pages={3758-70}
}
The ATP-dependent protein chaperone heat-shock protein 70 (Hsp70) displays broad anti-aggregation functions and has a critical function in preventing protein misfolding pathologies. According to in vitro and in vivo models of Parkinson's disease (PD), loss of Hsp70 activity is associated with neurodegeneration and the formation of amyloid deposits of alpha-synuclein (alphaSyn), which constitute the intraneuronal inclusions in PD patients known as Lewy bodies. Here, we show that Hsp70 depletion… CONTINUE READING