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

doi:10.1016/j.bbrc.2010.03.171

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 journal › Article › peer-review

25 Citations (Scopus)

Abstract

TREK1 belongs to a family of two-pore-domain K⁺ (K_2P) 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 language	English
Pages (from-to)	244-250
Number of pages	7
Journal	Biochemical and biophysical research communications
Volume	395
Issue number	2
DOIs	https://doi.org/10.1016/j.bbrc.2010.03.171
Publication status	Published - 2010 Apr 30
Externally published	Yes

Keywords

TREK1
Trafficking
Yeast two-hybrid screening
β-COP

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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10.1016/j.bbrc.2010.03.171

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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

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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",

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

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AU - Kim, Eunju

AU - Hwang, Eun Mi

AU - Yarishkin, Oleg

AU - Yoo, Jae Cheal

AU - Kim, Donggyu

AU - Park, Nammi

AU - Cho, Minhee

AU - Lee, Young Sun

AU - Sun, Choong Hyun

AU - Yi, Gwan Su

AU - Yoo, Jiyun

AU - Kang, Dawon

AU - Han, Jaehee

AU - Hong, Seong Geun

AU - Park, Jae Yong

PY - 2010/4/30

Y1 - 2010/4/30

N2 - 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

AB - 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

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KW - Trafficking

KW - Yeast two-hybrid screening

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

Abstract

Keywords

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