α-Synuclein binds extracellular complex N-linked glycans

摘要: Fibrillar deposits of α-Synuclein (αS) are the hallmark Parkinson9s disease. Recent evidence suggests that disease may propagate through cell-to-cell transmission toxic forms αS. Rele-vant to this mechanism, here we report discovery αS binds extracellular N-linked glycans. We find proteoliposomes derived from neuronal-lineage cells and removal glycans both decreases binding alters conformation bound Cellular internalization monomer fibrillar is specific reduced dramatically upon cleavage Our results suggest interactions with play an important role in cellular uptake relevant normal proteostasis as well pathogenic species.