A disulphide-linked heterodimer of TWIK-1 and TREK-1 mediates passive conductance in astrocytes

Title
A disulphide-linked heterodimer of TWIK-1 and TREK-1 mediates passive conductance in astrocytes
Authors
황은미김은주올레그우동호한경석박남미배연주우준성김동규박명기이창준박재용
Issue Date
2014-02
Publisher
Nature Communications
Citation
VOL 5, 3227-1-3227-15
Abstract
TWIK-1 is a member of the two-pore domain Kþ (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 cannabinoidinduced glutamate release from astrocytes. Our study sheds new light on the diversity of K2P channels.
URI
http://pubs.kist.re.kr/handle/201004/50216
ISSN
20411723
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