A disulphide-linked heterodimer of TWIK-1 and TREK-1 mediates passive conductance in astrocytes
- Authors
- Hwang, Eun Mi; Kim, Eunju; Yarishkin, Oleg; Woo, Dong Ho; Han, Kyung-Seok; Park, Nammi; Bae, Yeonju; Woo, Junsung; Kim, Donggyu; Park, Myeongki; Lee, C. Justin; Park, Jae-Yong
- Issue Date
- 2월-2014
- Publisher
- NATURE PUBLISHING GROUP
- Citation
- NATURE COMMUNICATIONS, v.5
- Indexed
- SCIE
SCOPUS
- Journal Title
- NATURE COMMUNICATIONS
- Volume
- 5
- URI
- https://scholar.korea.ac.kr/handle/2021.sw.korea/99430
- DOI
- 10.1038/ncomms4227
- ISSN
- 2041-1723
- Abstract
- TWIK-1 is a member of the two-pore domain K+ (K2P) channel family that plays an essential part in the regulation of resting membrane potential and cellular excitability. The physiological role of TWIK-1 has remained enigmatic because functional expression of TWIK-1 channels is elusive. Here we report that native TWIK-1 forms a functional channel at the plasma membrane of astrocytes. A search for TWIK-1-binding proteins led to the identification of TREK-1, another member of the K2P family. The TWIK-1/TREK-1 heterodimeric channel is formed via a disulphide bridge between residue C69 in TWIK-1 and C93 in TREK-1. Gene silencing demonstrates that surface expression of TWIK-1 and TREK-1 are interdependent. TWIK-1/TREK-1 heterodimers mediate astrocytic passive conductance and cannabinoid-induced glutamate release from astrocytes. Our study sheds new light on the diversity of K2P channels.
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Collections - Graduate School > KU-KIST Graduate School of Converging Science and Technology > 1. Journal Articles
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