ArticleThe Biochemical journal2009
Doppel and PrPC co-immunoprecipitate in detergent-resistant membrane domains of epithelial FRT cells.
Article in The Biochemical journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 20 citations in OpenAlex.
- Melatonin: Regulation of Prion Protein Phase Separation in Cancer Multidrug Resistance.Molecules (Basel, Switzerland) · 2022Review
- Cannabinoid receptors distribution in mouse cortical plasma membrane compartments.Molecular brain · 2021Article
- Prion Protein in Stem Cells: A Lipid Raft Component Involved in the Cellular Differentiation Process.International journal of molecular sciences · 2020Review
- APP Maturation and Intracellular Localization Are Controlled by a Specific Inhibitor of 37/67 kDa Laminin-1 Receptor in Neuronal Cells.International journal of molecular sciences · 2020Article
- Microbiome Influence in the Pathogenesis of Prion and Alzheimer's Diseases.International journal of molecular sciences · 2019Review
- Regulation of sub-compartmental targeting and folding properties of the Prion-like protein Shadoo.Scientific reports · 2017Article
- Physiological Functions of the Cellular Prion Protein.Frontiers in molecular biosciences · 2017Review
- Negative purifying selection drives prion and doppel protein evolution.Journal of molecular evolution · 2014Article
- Ataxia with cerebellar lesions in mice expressing chimeric PrP-Dpl protein.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2013Article
- Differential responses of neuronal and spermatogenic cells to the doppel cytotoxicity.PloS one · 2013Article
- The ZIP5 ectodomain co-localizes with PrP and may acquire a PrP-like fold that assembles into a dimer.PloS one · 2013Article
- Article
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
Abstract
Dpl (doppel) is a paralogue of the PrPC (cellular prion protein), whose misfolded conformer (the scrapie prion protein, PrPSc) is responsible for the onset of TSEs (transmissible spongiform encephalopathies) or prion diseases. It has been shown that the ectopic expression of Dpl in the brains of some lines of PrP-knockout mice provokes cerebellar ataxia, which can be rescued by the reintroduction of the PrP gene, suggesting a functional interaction between the two proteins. It is, however, still unclear where, and under which conditions, this event may occur. In the present study we addressed this issue by analysing the intracellular localization and the interaction between Dpl and PrPC in FRT (Fischer rat thyroid) cells stably expressing the two proteins separately or together. We show that both proteins localize prevalently on the basolateral surface of FRT cells, in both singly and doubly transfected clones. Interestingly we found that they associate with DRMs (detergent-resistant membranes) or lipid rafts, from where they can be co-immunoprecipitated in a cholesterol-dependent fashion. Although the interaction between Dpl and PrPC has been suggested before, our results provide the first clear evidence that this interaction occurs in rafts and is dependent on the integrity of these membrane microdomains. Furthermore, both Dpl and PrPC could be immunoprecipitated with flotillin-2, a raft protein involved in endocytosis and cell signalling events, suggesting that they share the same lipid environment.
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Registered trials
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