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@ARTICLE{Miesbauer:136016,
      author       = {Miesbauer, Margit and Rambold, Angelika S and Winklhofer,
                      Konstanze F and Tatzelt, Jörg},
      title        = {{T}argeting of the prion protein to the cytosol: mechanisms
                      and consequences.},
      journal      = {Current issues in molecular biology},
      volume       = {12},
      number       = {2},
      issn         = {1467-3037},
      address      = {Wymondham, Norfolk},
      reportid     = {DZNE-2020-02338},
      pages        = {10.21775/cimb.012.109},
      year         = {2010},
      abstract     = {Prion diseases are characterized by the conformational
                      transition of the cellular prion protein (PrP(C)) into an
                      aberrant protein conformer, designated scrapie-prion protein
                      (PrP(Sc)). A causal link between protein misfolding and
                      neurodegeneration has been established for a variety of
                      neurodegenerative disease, such as Alzheimer's disease,
                      Parkinson's disease and polyglutamine diseases, but there is
                      an ongoing debate about the nature of the neurotoxic species
                      and how non-native conformers can damage neuronal
                      populations. PrP is normally imported into the endoplasmic
                      reticulum (ER) and targeted to the outer leaflet of the
                      plasma membrane via a glycosylphosphatidylinositol (GPI)
                      anchor. However, several conditions, such as ER stress or
                      some pathogenic mutations in the PrP gene, can induce the
                      mislocalization of PrP in the cytosol, where it has a
                      neurotoxic potential as demonstrated in cell culture and
                      transgenic mouse models. In this review we focus on
                      intrinsic factors and cellular pathways implicated in the
                      import of PrP into the ER and its mistargeting to the
                      cytosol. The findings summarized here not only reveal a
                      complex regulation of the biogenesis of PrP, but also
                      provide interesting new insight into toxic activities of
                      pathogenic protein conformers and quality control pathways
                      of ER-targeted proteins.},
      subtyp        = {Review Article},
      keywords     = {Animals / Cytosol: metabolism / Endoplasmic Reticulum:
                      metabolism / Glycosylphosphatidylinositols: metabolism /
                      Humans / Models, Biological / Prion Diseases: genetics /
                      Prion Diseases: metabolism / Prions: genetics / Prions:
                      metabolism / Protein Transport: genetics / Protein
                      Transport: physiology / Glycosylphosphatidylinositols (NLM
                      Chemicals) / Prions (NLM Chemicals)},
      cin          = {Ext AG Tatzelt},
      ddc          = {570},
      cid          = {I:(DE-2719)5000053},
      pnm          = {342 - Disease Mechanisms and Model Systems (POF3-342)},
      pid          = {G:(DE-HGF)POF3-342},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:19767654},
      url          = {https://pub.dzne.de/record/136016},
}