Fibril-induced glutamine-/asparagine-rich prions recruit stress granule proteins in mammalian cells.

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 Sacchar

SUBMITTER: Riemschoss K 

PROVIDER: S-EPMC6607448 | biostudies-literature | 2019 Aug

REPOSITORIES: biostudies-literature