Abstract
Cell-to-cell transmission of toxic forms of α-Synuclein (αS) is thought to underlie disease progression in Parkinson's disease and other synucleinopathies. My lab identified a neuronal protein, neurexin 1β, as capable of driving selective uptake of αS; the interaction is dependent upon N-terminal aceylation of αS, as well as N-linked glycosylation of neurexin 1β. I will describe our efforts both to understand the role of N-terminal acetylation in αS binding to neurexin 1β as well as to determine whether this modification alters its interactions with other putative cellular binding partners. To do this, we use a variety of biophysical and quantitative cell biological methods. Our work provides insight into molecular details of the interaction between αS and neurexin 1β and whether this interaction may be exploited for therapeutic development.
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