Katerina Melachroinou

TL;DR: The results show for the first time that cell-produced α- Synuclein is secreted via an exosomal, calcium-dependent mechanism and suggest that α-synuclein secretion serves to amplify and propagate Parkinson's disease-related pathology.

TL;DR: It is shown that application of secreted AS alters membrane fluidity and increases calcium (Ca2+) entry and this influx is reduced on pharmacological inhibition of voltage-operated Ca2+ channels, suggesting that AS exerts toxicity through engagement, at least in part, of theCa2+ homeostatic machinery.

TL;DR: The data suggest that pS129 occurred subsequent to initial α-syn aggregation, lessened aggregation propensity, and attenuated cytotoxicity through diverse assays, and these findings highlight major implications for a better understanding of the role of a molecular modification on protein aggregation.

TL;DR: This work mapped for the first time the domain within LRRK2 that mediates the interaction with FADD, thereby activating the molecular machinery of the extrinsic death pathway and identifies multiple novel points within neuronal death signaling pathways that could potentially be targeted by candidate therapeutic strategies.

TL;DR: There is a critical need for sensitive and quantitative assays of leucine‐rich repeat kinase 2 function and target engagement.