Enhancement of TREK1 channel surface expression by protein-protein interaction with β-COP

Eunju Kim, Eun Mi Hwang, Oleg Yarishkin, Jae Cheal Yoo, Donggyu Kim, Nammi Park, Minhee Cho, Young Sun Lee, Choong Hyun Sun, Gwan Su Yi, Jiyun Yoo, Dawon Kang, Jaehee Han, Seong Geun Hong, Jae Yong Park

Research output: Contribution to journalArticle

19 Citations (Scopus)

Abstract

TREK1 belongs to a family of two-pore-domain K+ (K2P) channels and produce background currents that regulate cell excitability. In the present study, we identified a vesicle transport protein, β-COP, as an interacting partner by yeast two-hybrid screening of a human brain cDNA library with N-terminal region of TREK1 (TREK1-N) as bait. Several in vitro and in vivo binding assays confirmed the protein-protein interaction between TREK1 and β-COP. We also found that β-COP was associated with TREK1 in native condition at the PC3 cells. When RFP-β-COP was co-transfected with GFP-TREK1 into COS-7 cells, both proteins were found localized to the plasma membrane. In addition, the channel activity and surface expression of GFP-TREK1 increased dramatically by co-transfection with RFP-β-COP. Surface expression of the TREK1 channel was also clearly reduced with the addition of β-COP-specific shRNA. Collectively, these data suggest that β-COP plays a critical role in the forward transport of TREK1 channel to the plasma membrane. Crown

Original languageEnglish
Pages (from-to)244-250
Number of pages7
JournalBiochemical and biophysical research communications
Volume395
Issue number2
DOIs
Publication statusPublished - 2010 Apr 30
Externally publishedYes

Keywords

  • TREK1
  • Trafficking
  • Yeast two-hybrid screening
  • β-COP

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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  • Cite this

    Kim, E., Hwang, E. M., Yarishkin, O., Yoo, J. C., Kim, D., Park, N., Cho, M., Lee, Y. S., Sun, C. H., Yi, G. S., Yoo, J., Kang, D., Han, J., Hong, S. G., & Park, J. Y. (2010). Enhancement of TREK1 channel surface expression by protein-protein interaction with β-COP. Biochemical and biophysical research communications, 395(2), 244-250. https://doi.org/10.1016/j.bbrc.2010.03.171