Please use this identifier to cite or link to this item: https://doi.org/10.1016/j.jbc.2021.100359
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dc.titleCytoskeleton-dependent clustering of membrane-bound prion protein on the cell surface
dc.contributor.authorHackl, Stefanie
dc.contributor.authorNg, Xue Wen
dc.contributor.authorLu, Danqin
dc.contributor.authorWohland, Thorsten
dc.contributor.authorBecker, Christian F. W.
dc.date.accessioned2022-10-12T08:12:20Z
dc.date.available2022-10-12T08:12:20Z
dc.date.issued2021-01-01
dc.identifier.citationHackl, Stefanie, Ng, Xue Wen, Lu, Danqin, Wohland, Thorsten, Becker, Christian F. W. (2021-01-01). Cytoskeleton-dependent clustering of membrane-bound prion protein on the cell surface. Journal of Biological Chemistry 296 : 100359. ScholarBank@NUS Repository. https://doi.org/10.1016/j.jbc.2021.100359
dc.identifier.issn0021-9258
dc.identifier.urihttps://scholarbank.nus.edu.sg/handle/10635/232550
dc.description.abstractPrion diseases are a group of neurodegenerative disorders that infect animals and humans with proteinaceous particles called prions. Prions consist of scrapie prion protein (PrPSc), a misfolded version of the cellular prion protein (PrPC). During disease progression, PrPSc replicates by interacting with PrPC and inducing its conversion to PrPSc. Attachment of PrPC to cellular membranes via a glycosylphosphatidylinositol (GPI) anchor is critical for the conversion of PrPC into PrPSc. However, the mechanisms governing PrPC conversion and replication on the membrane remain largely unclear. Here, a siteselectively modified PrP variant equipped with a fluorescent GPI anchor mimic (PrP-GPI) was employed to directly observe PrP at the cellular membrane in neuronal SH-SY5Y cells. PrP-GPI exhibits a cholesterol-dependent membrane accumulation and a cytoskeleton-dependent mobility. More specifically, inhibition of actin polymerization reduced the diffusion of PrPGPI indicating protein clustering, which resembles the initial step of PrP aggregation and conversion into its pathogenic isoform. An intact actin cytoskeleton might therefore prevent conversion of PrPC into PrPSc and offer new therapeutic angles. © 2021 The Authors.
dc.publisherAmerican Society for Biochemistry and Molecular Biology Inc.
dc.rightsAttribution 4.0 International
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/
dc.sourceScopus OA2021
dc.typeArticle
dc.contributor.departmentDEPT OF BIOMEDICAL ENGINEERING
dc.contributor.departmentOFFICE OF THE DEPUTY PRESIDENT(RES&TECH)
dc.description.doi10.1016/j.jbc.2021.100359
dc.description.sourcetitleJournal of Biological Chemistry
dc.description.volume296
dc.description.page100359
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