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- W3023343670 abstract "Significance Direct cell-to-cell spreading of misfolded protein aggregates, such as α-synuclein fibrils (α-Syn), is a pathological hallmark associated with the progression of many neurodegenerative diseases, but it is unclear how mammalian cells take up large protein aggregates to initiate this prion-like protein transmission process. Here we define the endocytosis mechanism of α-Syn preformed fibrils (PFFs) using a combination of genetic, biochemical, and live-cell imaging techniques. Our study shows that α-Syn PFFs enter cells following an entry pathway that is specifically tailored for cargos bearing positive charges. These cargos bind to heparan sulfate proteoglycans on the cell surface via charge–charge interactions, which enable cargo internalization by a previously unknown endocytosis mechanism that requires forces generated by myosin-7B and actin filaments." @default.
- W3023343670 created "2020-05-13" @default.
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- W3023343670 date "2020-05-04" @default.
- W3023343670 modified "2023-10-10" @default.
- W3023343670 title "A myosin-7B–dependent endocytosis pathway mediates cellular entry of α-synuclein fibrils and polycation-bearing cargos" @default.
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- W3023343670 doi "https://doi.org/10.1073/pnas.1918617117" @default.
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