ArticleNature communications2013
Prions disturb post-Golgi trafficking of membrane proteins.
Article in Nature communications, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 62 citations in OpenAlex.
- The Role of the Golgi Apparatus in Neurodegeneration.Sub-cellular biochemistry · 2026Review
- The dynamics of prion spreading is governed by the interplay between the non-linearities of tissue response and replication kinetics.iScience · 2024Article
- Protective role of cytosolic prion protein against virus infection in prion-infected cells.Journal of virology · 2024Article
- Full-length prion protein incorporated into prion aggregates is a marker for prion strain-specific destabilization of aggregate structure following cellular uptake.Journal of biochemistry · 2023Article
- Cholesterol and its reciprocal association with prion infection.Cell and tissue research · 2023Review
- Prion Pathogenesis Revealed in a Series of the Special Issues "Prions and Prion Diseases".International journal of molecular sciences · 2022Article
- What is the role of lipids in prion conversion and disease?Frontiers in molecular neuroscience · 2022Review
- A New Take on Prion Protein Dynamics in Cellular Trafficking.International journal of molecular sciences · 2020Review
- Strain-Dependent Prion Infection in Mice Expressing Prion Protein with Deletion of Central Residues 91-106.International journal of molecular sciences · 2020Article
- The Role of Vesicle Trafficking Defects in the Pathogenesis of Prion and Prion-Like Disorders.International journal of molecular sciences · 2020Review
- Identification of circulating microRNA signatures as potential biomarkers in the serum of elk infected with chronic wasting disease.Scientific reports · 2019Article
- RNA editing alterations define manifestation of prion diseases.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Analysis of RNA Expression Profiles Identifies Dysregulated Vesicle Trafficking Pathways in Creutzfeldt-Jakob Disease.Molecular neurobiology · 2019Article
- Review
- Attempt to Untangle the Prion-Like Misfolding Mechanism for Neurodegenerative Diseases.International journal of molecular sciences · 2018Review
- Prions amplify through degradation of the VPS10P sorting receptor sortilin.PLoS pathogens · 2017Article
- Exosomes and the Prion Protein: More than One Truth.Frontiers in neuroscience · 2017Review
- Prion protein inhibits fast axonal transport through a mechanism involving casein kinase 2.PloS one · 2017Article
- Two PTP receptors mediate CSPG inhibition by convergent and divergent signaling pathways in neurons.Scientific reports · 2016Article
- Misfolding leads the way to unraveling signaling pathways in the pathophysiology of prion diseases.Prion · 2016Review
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Conformational conversion of normal cellular prion protein PrP(C) into pathogenic PrP(Sc) is central to the pathogenesis of prion diseases. However, the pathogenic mechanism remains unknown. Here we show that post-Golgi vesicular trafficking is significantly delayed in prion-infected N2a cells. Accordingly, cell surface expression of membrane proteins examined, including PrP(C), insulin receptor involved in neuroprotection, and attractin, whose mutation causes prion disease-like spongiform neurodegeneration, is reduced. Instead, they accumulate in the Golgi apparatus. PrP(Sc) is detected throughout endosomal compartments, being particularly abundant in recycling endosome. We also show reduced surface expression of PrP(C) and insulin receptor in prion-infected mouse brains well before the onset of disease. These results suggest that prion infection might impair post-Golgi trafficking of membrane proteins to the cell surface in neurons via PrP(Sc) accumulated in recycling endosome, and eventually induce neuronal dysfunctions associated with prion diseases.
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