ArticleThe Journal of biological chemistry2014
A C-terminal membrane anchor affects the interactions of prion proteins with lipid membranes.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 31 citations in OpenAlex.
- Segmental Isotope Labeling of the Prion Protein: Identification of a Key Residue for Copper-Mediated Interdomain Structure.ACS chemical biology · 2025Article
- Chemische Synthese und Semisynthese von lipidierten Proteinen.Angewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2022Review
- Chemical Synthesis and Semisynthesis of Lipidated Proteins.Angewandte Chemie (International ed. in English) · 2022Review
- What is the role of lipids in prion conversion and disease?Frontiers in molecular neuroscience · 2022Review
- Chemoenzymatic Semisynthesis of Proteins.Chemical reviews · 2020Review
- Prion protein-Semisynthetic prion protein (PrP) variants with posttranslational modifications.Journal of peptide science : an official publication of the European Peptide Society · 2019Review
- Prion neurotoxicity.Brain pathology (Zurich, Switzerland) · 2019Review
- Article
- Chemical synthesis of membrane proteins: a model study on the influenza virus B proton channel.Chemical science · 2018Article
- Utility of the Phenacyl Protecting Group in Traceless Protein Semisynthesis through Ligation-Desulfurization Chemistry.ChemistryOpen · 2018Article
- Semisynthetic prion protein (PrP) variants carrying glycan mimics at position 181 and 197 do not form fibrils.Chemical science · 2017Article
- The prion protein family member Shadoo induces spontaneous ionic currents in cultured cells.Scientific reports · 2016Article
- The Pathogenic A116V Mutation Enhances Ion-Selective Channel Formation by Prion Protein in Membranes.Biophysical journal · 2016Article
- Expression of the Prion Protein Family Member Shadoo Causes Drug Hypersensitivity That Is Diminished by the Coexpression of the Wild Type Prion Protein.The Journal of biological chemistry · 2016Article
- Prion 2016 Poster Abstracts.Prion · 2016Article
- Cytoskeleton-dependent clustering of membrane-bound prion protein on the cell surface.The Journal of biological chemistryArticle
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
Membrane attachment via a C-terminal glycosylphosphatidylinositol anchor is critical for conversion of PrP(C) into pathogenic PrP(Sc). Therefore the effects of the anchor on PrP structure and function need to be deciphered. Three PrP variants, including full-length PrP (residues 23-231, FL_PrP), N-terminally truncated PrP (residues 90-231, T_PrP), and PrP missing its central hydrophobic region (Δ105-125, ΔCR_PrP), were equipped with a C-terminal membrane anchor via a semisynthesis strategy. Analyses of the interactions of lipidated PrPs with phospholipid membranes demonstrated that C-terminal membrane attachment induces a different binding mode of PrP to membranes, distinct from that of non-lipidated PrPs, and influences the biochemical and conformational properties of PrPs. Additionally, fluorescence-based assays indicated pore formation by lipidated ΔCR_PrP, a variant that is known to be highly neurotoxic in transgenic mice. This finding was supported by using patch clamp electrophysiological measurements of cultured cells. These results provide new evidence for the role of the membrane anchor in PrP-lipid interactions, highlighting the importance of the N-terminal and the central hydrophobic domain in these interactions.
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Registered trials
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.