| Literature DB >> 24496152 |
Eun Mi Hwang1, Eunju Kim2, Oleg Yarishkin3, Dong Ho Woo4, Kyung-Seok Han4, Nammi Park5, Yeonju Bae3, Junsung Woo4, Donggyu Kim5, Myeongki Park4, C Justin Lee6, Jae-Yong Park7.
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.Entities:
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Year: 2014 PMID： 24496152 DOI： 10.1038/ncomms4227
Source DB: PubMed Journal: Nat Commun ISSN： 2041-1723 Impact factor: 14.919