ArticlePrion
Trafficking of PrPc to mitochondrial raft-like microdomains during cell apoptosis.
Article in Prion. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed.
- Synaptic-mitochondrial transport: mechanisms in neural adaptation and degeneration.Molecular and cellular biochemistry · 2025Review
- Extracellular Vesicles in the Crosstalk of Autophagy and Apoptosis: A Role for Lipid Rafts.Cells · 2025Review
- Physiology of Cellular Prion Proteins in Reproduction.Development & reproduction · 2024Article
- Article
- Methodological Pitfalls of Investigating Lipid Rafts in the Brain: What Are We Still Missing?Biomolecules · 2024Review
- Roles of prion proteins in mammalian development.Animal cells and systems · 2024Review
- Different Chronic Stress Paradigms Converge on Endogenous TDP43 Cleavage and Aggregation.Molecular neurobiology · 2023Article
- Lipid rafts mediate multilineage differentiation of human dental pulp-derived stem cells (DPSCs).Frontiers in cell and developmental biology · 2023Article
- Gangliosides and Their Role in Multilineage Differentiation of Mesenchymal Stem Cells.Biomedicines · 2022Review
- Article
- Article
- Connection Lost, MAM: Errors in ER-Mitochondria Connections in Neurodegenerative Diseases.Brain sciences · 2021Review
- Cellular Prion Protein (PrPc): Putative Interacting Partners and Consequences of the Interaction.International journal of molecular sciences · 2020Review
- Cellular and Molecular Mechanisms Mediated by recPrPInternational journal of molecular sciences · 2019Article
- Lipids in the cell: organisation regulates function.Cellular and molecular life sciences : CMLS · 2018Review
- Article
- Cellular prion protein is present in mitochondria of healthy mice.Scientific reports · 2017Article
- Physiological Functions of the Cellular Prion Protein.Frontiers in molecular biosciences · 2017Review
- Article
- Losing sleep over mitochondria: a new player in the pathophysiology of fatal familial insomnia.Brain pathology (Zurich, Switzerland) · 2017Article
Corrections and comments
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The cellular form of prion protein (PrP (c)) is a highly conserved cell surface GPI-anchored glycoprotein that was identified in cholesterol-enriched, detergent-resistant microdomains, named "rafts." The association with these specialized portions of the cell plasma membrane is required for conversion of PrP (c) to the transmissible spongiform encephalopathy-associated protease-resistant isoform. Usually, PrP (c) is reported to be a plasma membrane protein, however several studies have revealed PrP (c) as an interacting protein mainly with the membrane/organelles, as well as with cytoskeleton network. Recent lines of evidence indicated its association with ER lipid raft-like microdomains for a correct folding of PrP (c), as well as for the export of the protein to the Golgi and proper glycosylation. During cell apoptosis, PrP (c) can undergo intracellular re-localization, via ER-mitochondria associated membranes (MAM) and microtubular network, to mitochondrial raft-like microdomains, where it induced the loss of mitochondrial membrane potential and citochrome c release, after a contained raise of calcium concentration. We suggest that PrP (c) may play a role in the multimolecular signaling complex associated with cell apoptosis Lipid rafts and their components may, thus, be investigated as pharmacological targets of interest, introducing a novel and innovative task in modern pharmacology, i.e., the development of glycosphingolipid targeted drugs.
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