Enhancement of TREK1 channel surface expression by protein–protein interaction with β-COP
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- 作者：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 Pa
- 关键词：TREK1 ; β ; -COP ; Yeast two-hybrid screening ; Trafficking
- 刊名：Biochemical and Biophysical Research Communications
- 出版年：2010
- 出版时间：30 April 2010
- 年：2010
- 卷：395
- 期：2
- 页码：244-250
- 全文大小：609 K
文摘
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.