The number of α-synuclein proteins per vesicle gives insights into its physiological function

Mohammad Amin Abolghassemi Fakhree, Niels Zijlstra, Christian C. Raiss, Remco Siero, H. Grabmayr, A.R. Bausch, Christian Blum, Mireille M.A.E. Claessens

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Although it is well established that the protein α-synuclein (αS) plays an important role in Parkinson’s disease, its physiological function remains largely unknown. It has been reported to bind membranes and to play a role in membrane remodeling processes. The mechanism by which αS remodels membranes is still debated; it may either affect its physical properties or act as a chaperone for other membrane associated proteins. To obtain insight into the role of αS in membrane remodeling we investigated the number of αS proteins associated with single small vesicles in a neuronal cell model. Using single-molecule microscopy and photo-bleaching approaches, we most frequently found 70 αS-GFPs per vesicle. Although this number is high enough to modulate physical membrane properties, it is also strikingly similar to the number of synaptobrevins, a putative interaction partner of αS, per vesicle. We therefore hypothesize a dual, synergistic role for αS in membrane remodeling
Original languageEnglish
Article number30658
JournalScientific reports
Issue number30658
Publication statusPublished - 2016


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