Abstract
Department of Chemistry, Sejong University, Seoul 143-747, KoreaReceived May 16, 2012, Accepted June 26, 2012Human α-synuclein is the major component of the protein aggregates known as Lewy bodies or Lewy neurites,which define the intracellular lesions of Parkinson’s disease. Despite extensive efforts, the physiologicalfunction of α-synuclein has not yet been elucidated in detail. As an approach to defining its function, proteinsthat interacted with α-synuclein were screened in phage display assays. The SNARE protein vesicle t-SNARE-interacting protein homologous 1B (VTI1B) was identified as an interacting partner. A selective interactionbetween α-synuclein and VTI1B was confirmed by coimmunoprecipitation and GST pull-down assays. VTI1Band α-synuclein were colocalized in N2a neuronal cells, and overexpression of α-synuclein changed thesubcellular localization of VTI1B to be more dispersed throughout the cytosol. Considering the role played byVTI1B, α-synuclein is likely to modulate vesicle trafficking by interacting with a SNARE complex.Key Words : α-Synuclein, Protein interaction, VTI1B, Vesicle traffickingIntroductionThe mutation (A30P, A53T and E46K) or overexpression(duplication and triplication) of α-synuclein causes someforms of familial PD Parkinson’s disease (PD).
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