A disulphide-linked heterodimer of TWIK-1 and TREK-1 mediates passive conductance in astrocytes
- A disulphide-linked heterodimer of TWIK-1 and TREK-1 mediates passive conductance in astrocytes
- 황은미; 김은주; 올레그; 우동호; 한경석; 박남미; 배연주; 우준성; 김동규; 박명기; 이창준; 박재용
- Issue Date
- Nature Communications
- VOL 5, 3227-1-3227-15
- 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.
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