Fernández Busnadiego, Rubén

[["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Nature Communications"],["dc.bibliographiccitation.volume","12"],["dc.contributor.author","Trinkaus, Victoria A."],["dc.contributor.author","Riera-Tur, Irene"],["dc.contributor.author","Martínez-Sánchez, Antonio"],["dc.contributor.author","Bäuerlein, Felix J. B."],["dc.contributor.author","Guo, Qiang"],["dc.contributor.author","Arzberger, Thomas"],["dc.contributor.author","Baumeister, Wolfgang"],["dc.contributor.author","Dudanova, Irina"],["dc.contributor.author","Hipp, Mark S."],["dc.contributor.author","Fernández Busnadiego, Rubén"],["dc.date.accessioned","2021-06-01T09:41:39Z"],["dc.date.available","2021-06-01T09:41:39Z"],["dc.date.issued","2021"],["dc.description.abstract","Abstract The molecular architecture of α-Synuclein (α-Syn) inclusions, pathognomonic of various neurodegenerative disorders, remains unclear. α-Syn inclusions were long thought to consist mainly of α-Syn fibrils, but recent reports pointed to intracellular membranes as the major inclusion component. Here, we use cryo-electron tomography (cryo-ET) to image neuronal α-Syn inclusions in situ at molecular resolution. We show that inclusions seeded by α-Syn aggregates produced recombinantly or purified from patient brain consist of α-Syn fibrils crisscrossing a variety of cellular organelles. Using gold-labeled seeds, we find that aggregate seeding is predominantly mediated by small α-Syn fibrils, from which cytoplasmic fibrils grow unidirectionally. Detailed analysis of membrane interactions revealed that α-Syn fibrils do not contact membranes directly, and that α-Syn does not drive membrane clustering. Altogether, we conclusively demonstrate that neuronal α-Syn inclusions consist of α-Syn fibrils intermixed with membranous organelles, and illuminate the mechanism of aggregate seeding and cellular interaction."],["dc.identifier.doi","10.1038/s41467-021-22108-0"],["dc.identifier.pmid","33854052"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/84996"],["dc.identifier.url","https://mbexc.uni-goettingen.de/literature/publications/276"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-425"],["dc.relation","EXC 2067: Multiscale Bioimaging"],["dc.relation.eissn","2041-1723"],["dc.relation.workinggroup","RG Fernández-Busnadiego (Structural Cell Biology)"],["dc.rights","CC BY 4.0"],["dc.title","In situ architecture of neuronal α-Synuclein inclusions"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]