Bulletin of the Korean Chemical Society

Korean Chemical Society (대한화학회)
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Interaction of Human α-Synuclein with VTI1B May Modulate Vesicle Trafficking

  • Lee, Hak-Joo (Department of Molecular Biology, Sejong University) ;
  • Lee, Kyung-Hee (Department of Chemistry, Sejong University) ;
  • Im, Ha-Na (Department of Molecular Biology, Sejong University)
  • Received : 2012.05.16
  • Accepted : 2012.06.26
  • Published : 2012.09.20
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Abstract

Human ${\alpha}$-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 physiological function of ${\alpha}$-synuclein has not yet been elucidated in detail. As an approach to defining its function, proteins that interacted with ${\alpha}$-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 interaction between ${\alpha}$-synuclein and VTI1B was confirmed by coimmunoprecipitation and GST pull-down assays. VTI1B and ${\alpha}$-synuclein were colocalized in N2a neuronal cells, and overexpression of ${\alpha}$-synuclein changed the subcellular localization of VTI1B to be more dispersed throughout the cytosol. Considering the role played by VTI1B, ${\alpha}$-synuclein is likely to modulate vesicle trafficking by interacting with a SNARE complex.

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References

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