ArticlePloS one2008
Pathologic prion protein infects cells by lipid-raft dependent macropinocytosis.
Article in PloS one, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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Who cites it
40 citing papers in PubMed, 72 citations in OpenAlex.
- Extracellular vesicles in metabolic dysfunction-associated steatotic liver disease: From intercellular signaling to clinical translation.World journal of hepatology · 2025Review
- Sciatic Integrity Is Necessary for Fast and Efficient Scrapie Infection After Footpad Injection.International journal of molecular sciences · 2025Article
- Prion Protein Endoproteolysis: Cleavage Sites, Mechanisms and Connections to Prion Disease.Journal of neurochemistry · 2025Review
- Neuronal Ndst1 depletion accelerates prion protein clearance and slows neurodegeneration in prion infection.PLoS pathogens · 2023Article
- A review of the regulatory mechanisms of extracellular vesicles-mediated intercellular communication.Cell communication and signaling : CCS · 2023Review
- Cell biology of prion strains in vivo and in vitro.Cell and tissue research · 2023Review
- Biological Functions of the Intrinsically Disordered N-Terminal Domain of the Prion Protein: A Possible Role of Liquid-Liquid Phase Separation.Biomolecules · 2021Review
- A New Take on Prion Protein Dynamics in Cellular Trafficking.International journal of molecular sciences · 2020Review
- Cellular evasion strategies of Helicobacter pylori in regulating its intracellular fate.Seminars in cell & developmental biology · 2020Review
- Prion neurotoxicity.Brain pathology (Zurich, Switzerland) · 2019Review
- Advances in intracellular delivery through supramolecular self-assembly of oligonucleotides and peptides.Theranostics · 2019Review
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- Therapeutic effect of transmembrane TAT-tCNTF via Erk and Akt activation usingInternational journal of clinical and experimental pathology · 2018Article
- Article
- Prion strains depend on different endocytic routes for productive infection.Scientific reports · 2017Article
- Article
- Extracellular vesicles in neurodegenerative disease - pathogenesis to biomarkers.Nature reviews. Neurology · 2016Review
- Prions and Protein Assemblies that Convey Biological Information in Health and Disease.Neuron · 2016Review
- SOD1 protein aggregates stimulate macropinocytosis in neurons to facilitate their propagation.Molecular neurodegeneration · 2015Article
- Tau Trimers Are the Minimal Propagation Unit Spontaneously Internalized to Seed Intracellular Aggregation.The Journal of biological chemistry · 2015Article
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Transmissible spongiform encephalopathies, including variant-Creutzfeldt-Jakob disease (vCJD) in humans and bovine spongiform encephalopathies in cattle, are fatal neurodegenerative disorders characterized by protein misfolding of the host cellular prion protein (PrP(C)) to the infectious scrapie form (PrP(Sc)). However, the mechanism that exogenous PrP(Sc) infects cells and where pathologic conversion of PrP(C) to the PrP(Sc) form occurs remains uncertain. Here we report that similar to the mechanism of HIV-1 TAT-mediated peptide transduction, processed mature, full length PrP contains a conserved N-terminal cationic domain that stimulates cellular uptake by lipid raft-dependent, macropinocytosis. Inhibition of macropinocytosis by three independent means prevented cellular uptake of recombinant PrP; however, it did not affect recombinant PrP cell surface association. In addition, fusion of the cationic N-terminal PrP domain to a Cre recombinase reporter protein was sufficient to promote both cellular uptake and escape from the macropinosomes into the cytoplasm. Inhibition of macropinocytosis was sufficient to prevent conversion of PrP(C) to the pathologic PrP(Sc) form in N2a cells exposed to strain RML PrP(Sc) infected brain homogenates, suggesting that a critical determinant of PrP(C) conversion occurs following macropinocytotic internalization and not through mere membrane association. Taken together, these observations provide a cellular mechanism that exogenous pathological PrP(Sc) infects cells by lipid raft dependent, macropinocytosis.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.