Early Delivery of Misfolded PrP from ER to Lysosomes by Autophagy

@inproceedings{Cortes2013EarlyDO,
  title={Early Delivery of Misfolded PrP from ER to Lysosomes by Autophagy},
  author={Constanza J. Cortes and Kefeng Qin and Eric M. Norstrom and William N Green and Vytautas P. Bindokas and James A. Mastrianni},
  booktitle={International journal of cell biology},
  year={2013}
}
Prion diseases are linked to the accumulation of a misfolded isoform (PrP(Sc)) of prion protein (PrP). Evidence suggests that lysosomes are degradation endpoints and sites of the accumulation of PrP(Sc). We questioned whether lysosomes participate in the early quality control of newly generated misfolded PrP. We found PrP carrying the disease-associated T182A mutation (Mut-PrP) was delivered to lysosomes in a Golgi-independent manner. Time-lapse live cell imaging revealed early formation and… CONTINUE READING
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Rapamycin delays disease onset and prevents PrP plaque deposition in amousemodel of gerstmannstrausslerscheinker disease

  • H. Lorenz E. Grasbon-Frodl, U. Mann, R. M. Nitsch, O. Windl, H. A. Kretzschmar
  • The Journal of Neuroscience
  • 2012

Sustained translational repression by eIF 2 alphaPmediates prion neurodegeneration

  • T. Verfaillie, M. Salazar, P. Agostinis
  • Nature
  • 2012

Sustained translational repression by eIF2alpha- Pmediates prion neurodegeneration,”Nature

  • J. A. Moreno
  • vol. 485,
  • 2012
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