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 2024-01-20T10:31:57Z 2024-01-20T10:31:57Z 2021-09-05 2014-02 2041-1723 https://pubs.kist.re.kr/handle/201004/127133 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. English NATURE PUBLISHING GROUP DOMAIN POTASSIUM CHANNELS BIMOLECULAR FLUORESCENCE COMPLEMENTATION PROTEIN-PROTEIN INTERACTIONS RECTIFYING K+ CHANNEL PLASMA-MEMBRANE LIVING CELLS INDUCED INHIBITION ION SELECTIVITY F-ACTIN LOCALIZATION A disulphide-linked heterodimer of TWIK-1 and TREK-1 mediates passive conductance in astrocytes Article 10.1038/ncomms4227 1 NATURE COMMUNICATIONS, v.5 NATURE COMMUNICATIONS 5 scie scopus 000332665700002 2-s2.0-84893844068 Multidisciplinary Sciences Science & Technology - Other Topics Article DOMAIN POTASSIUM CHANNELS BIMOLECULAR FLUORESCENCE COMPLEMENTATION PROTEIN-PROTEIN INTERACTIONS RECTIFYING K+ CHANNEL PLASMA-MEMBRANE LIVING CELLS INDUCED INHIBITION ION SELECTIVITY F-ACTIN LOCALIZATION