Physiological C-terminal truncation of α-synuclein potentiates the prion-like formation of pathological inclusions.

ABSTRACT: α-Synuclein (αsyn) aggregates into toxic fibrils in multiple neurodegenerative diseases where these fibrils form characteristic pathological inclusions such as Lewy bodies (LBs). The mechanisms initiating αsyn aggregation into fibrils are unclear, but ubiquitous post-translational modifications of αsyn present in LBs may play a role. Specific C-terminally (C)-truncated forms of αsyn are present within human pathological inclusions and form under physiological conditions likely in lysosome-associated pathways, but the roles for these C-truncated forms of αsyn in inclusion formation and disease are not well understood. Herein, we characterized the in vitro aggregation properties, amyloid fibril structures, and ability to induce full-length (FL) αsyn aggregation through prion-like mech

SUBMITTER: Sorrentino ZA 

PROVIDER: S-EPMC6295729 | biostudies-literature | 2018 Dec

REPOSITORIES: biostudies-literature