Synucleinopathies are a group of neurodegenerative disorders that share common pathological intracellular deposits that contain aggregates of the protein ┙-synuclein. Substantial evidence suggests that fibril formation by ┙-synuclein is a critical step in the development of Parkinson's disease (PD). Indeed, in vitro, ┙-synuclein forms fibrils with morphologies and staining characteristics similar to those extracted from disease-affected brains. Also, three single-point mutations and duplication or triplication of the ┙-synuclein locus correlate with early onset of PD. However, the function of ┙-synuclein remains unknown. A significant portion of ┙synuclein is localized within membrane fractions, and especially synaptic vesicles associated with vesicular transport processes. These observations suggest that ┙-synuclein has a role in vesicular trafficking. Although ┙-synuclein belongs to a group of natively unfolded proteins, there is strong evidence that the membrane affinity of the protein induces an ┙helical conformation. A large number of studies have investigated ┙-synuclein–lipid interactions in the search for a physiological function, as well as to understand this potential membrane involvement in the pathogenesis of ┙-synuclein. In this review, we will predominantly focus on current opinion about the native wild-type ┙-synuclein–lipid interactions and the structure of ┙-synuclein that is established at the membrane surface. However, it should be noted that membranes have been reported to both accelerate and inhibit the fibril formation of ┙-synuclein, although this will not be the focus of the present review.