Spreading of a prion domain from cell-to-cell by vesicular transport in Caenorhabditis elegans.

ABSTRACT: Prion proteins can adopt self-propagating alternative conformations that account for the infectious nature of transmissible spongiform encephalopathies (TSEs) and the epigenetic inheritance of certain traits in yeast. Recent evidence suggests a similar propagation of misfolded proteins in the spreading of pathology of neurodegenerative diseases including Alzheimer's or Parkinson's disease. Currently there is only a limited number of animal model systems available to study the mechanisms that underlie the cell-to-cell transmission of aggregation-prone proteins. Here, we have established a new metazoan model in Caenorhabditis elegans expressing the prion domain NM of the cytosolic yeast prion protein Sup35, in which aggregation and toxicity are dependent upon the length of oligopeptide repea

SUBMITTER: Nussbaum-Krammer CI 

PROVIDER: S-EPMC3610634 | biostudies-literature | 2013 Mar

REPOSITORIES: biostudies-literature