Fibril-induced glutamine-/asparagine-rich prions recruit stress granule proteins in mammalian cells
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- dc.contributor.author Riemschoss, Katrin
- dc.contributor.author Arndt, Verena
- dc.contributor.author Bolognesi, Benedetta
- dc.contributor.author von Eisenhart-Rothe, Philipp
- dc.contributor.author Liu, Shu
- dc.contributor.author Buravlova, Oleksandra
- dc.contributor.author Duernberger, Yvonne
- dc.contributor.author Paulsen, Lydia
- dc.contributor.author Hornberger, Annika
- dc.contributor.author Hossinger, André
- dc.contributor.author Lorenzo Gotor, Maria de las Nieves
- dc.contributor.author Hogl, Sebastian
- dc.contributor.author Müller, Stephan A.
- dc.contributor.author Tartaglia, Gian Gaetano
- dc.contributor.author Lichtenthaler, Stefan F.
- dc.contributor.author Vorberg, Ina M.
- dc.date.accessioned 2019-10-25T11:12:00Z
- dc.date.available 2019-10-25T11:12:00Z
- dc.date.issued 2019
- dc.description.abstract Prions of lower eukaryotes are self-templating protein aggregates that replicate by converting homotypic proteins into stable, tightly packed beta-sheet-rich protein assemblies. Propagation is mediated by prion domains, low-complexity regions enriched in polar and devoid of charged amino acid residues. In mammals, compositionally similar domains modulate the assembly of dynamic stress granules (SGs) that associate via multivalent weak interactions. Dysregulation of SGs composed of proteins with prion-like domains has been proposed to underlie the formation of pathological inclusions in several neurodegenerative diseases. The events that drive prion-like domains into transient or solid assemblies are not well understood. We studied the interactors of the prototype prion domain NM of Saccharomyces cerevisiae Sup35 in its soluble or fibril-induced prion conformation in the mammalian cytosol. We show that the interactomes of soluble and prionized NM overlap with that of SGs. Prion induction by exogenous seeds does not cause SG assembly, demonstrating that colocalization of aberrant protein inclusions with SG components does not necessarily reveal SGs as initial sites of protein misfolding.
- dc.format.mimetype application/pdf
- dc.identifier.citation Riemschoss K, Arndt V, Bolognesi B, von Eisenhart-Rothe P, Liu S, Buravlova O et al. Fibril-induced glutamine-/asparagine-rich prions recruit stress granule proteins in mammalian cells. Life Sci Alliance. 2019;2(4):e201800280. DOI: 10.26508/lsa.201800280
- dc.identifier.doi http://dx.doi.org/10.26508/lsa.201800280
- dc.identifier.issn 2575-1077
- dc.identifier.uri http://hdl.handle.net/10230/42509
- dc.language.iso eng
- dc.publisher Life Science Alliance
- dc.relation.ispartof Life Science Alliance. 2019;2(4):e201800280
- dc.rights © 2019 Riemschoss et al. This article is available under a Creative Commons License (Attribution 4.0 International, as described at https://creativecommons.org/licenses/by/4.0/).
- dc.rights.accessRights info:eu-repo/semantics/openAccess
- dc.rights.uri https://creativecommons.org/licenses/by/4.0/
- dc.title Fibril-induced glutamine-/asparagine-rich prions recruit stress granule proteins in mammalian cells
- dc.type info:eu-repo/semantics/article
- dc.type.version info:eu-repo/semantics/publishedVersion