Effects of phosphorylating α-syn at Thr64 and Thr72 in nerve terminals

Collectively, we demonstrate for the first time that the binding between alpha-synuclein and membranes can be regulated by phosphorylation by the kinase PKR, identifies the responsible phosphorylation sites, and demonstrates it can modulate the binding between two vesicles by favoring the “double anchor” vesicle-binding mode. Moreover, phosphorylation inhibits the pathological aggregation of alpha-synuclein in cells and brain tissue.