Journal
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume 395, Issue 2, Pages 244-250Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2010.03.171
Keywords
TREK1; beta-COP; Yeast two-hybrid screening; Trafficking
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Funding
- Korea Science & Engineering Foundation [R13-2005-012-02002-0]
- Korea Research Foundation [KRF-2006-005-J04204]
- Brain Korea 21 Programs
- National Research Foundation of Korea [R13-2005-012-02002-0, 2006-005-J04204] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
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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, beta-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 beta-COP. We also found that beta-cop was associated with TREK1 in native condition at the PC3 cells. When RFP-beta-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-beta-COP. Surface expression of the TREK1 channel was also clearly reduced with the addition of beta-COP-specific shRNA. Collectively, these data suggest that beta-COP plays a critical role in the forward transport of TREK1 channel to the plasma membrane. Crown Copyright (C) 2010 Published by Elsevier Inc. All rights reserved.
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