[HTML][HTML] Mutant PrP is delayed in its exit from the endoplasmic reticulum, but neither wild-type nor mutant PrP undergoes retrotranslocation prior to proteasomal …
B Drisaldi, RS Stewart, C Adles, LR Stewart… - Journal of Biological …, 2003 - ASBMB
The cellular mechanisms by which prions cause neurological dysfunction are poorly
understood. To address this issue, we have been using cultured cells to analyze the
localization, biosynthesis, and metabolism of PrP molecules carrying mutations associated
with familial prion diseases. We report here that mutant PrP molecules are delayed in their
maturation to an endoglycosidase H-resistant form after biosynthetic labeling, suggesting
that they are impaired in their exit from the endoplasmic reticulum (ER). However, we find …
understood. To address this issue, we have been using cultured cells to analyze the
localization, biosynthesis, and metabolism of PrP molecules carrying mutations associated
with familial prion diseases. We report here that mutant PrP molecules are delayed in their
maturation to an endoglycosidase H-resistant form after biosynthetic labeling, suggesting
that they are impaired in their exit from the endoplasmic reticulum (ER). However, we find …