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

Eun Mi Hwang, Eunju Kim, Oleg Yarishkin, Dong Ho Woo, Kyung-Seok Han, Nammi Park, Yeonju Bae, Junsung Woo, Donggyu Kim, Myeongki Park, C. Justin Lee () and Jae-Yong Park ()
Additional contact information
Eun Mi Hwang: Institute of Health Science and Medical Research Center for Neural Dysfunction, Gyeongsang National University School of Medicine
Eunju Kim: Institute of Health Science and Medical Research Center for Neural Dysfunction, Gyeongsang National University School of Medicine
Oleg Yarishkin: WCI Center for Functional Connectomics, Korea Institute of Science and Technology (KIST)
Dong Ho Woo: WCI Center for Functional Connectomics, Korea Institute of Science and Technology (KIST)
Kyung-Seok Han: WCI Center for Functional Connectomics, Korea Institute of Science and Technology (KIST)
Nammi Park: Institute of Health Science and Medical Research Center for Neural Dysfunction, Gyeongsang National University School of Medicine
Yeonju Bae: WCI Center for Functional Connectomics, Korea Institute of Science and Technology (KIST)
Junsung Woo: WCI Center for Functional Connectomics, Korea Institute of Science and Technology (KIST)
Donggyu Kim: Institute of Health Science and Medical Research Center for Neural Dysfunction, Gyeongsang National University School of Medicine
Myeongki Park: WCI Center for Functional Connectomics, Korea Institute of Science and Technology (KIST)
C. Justin Lee: WCI Center for Functional Connectomics, Korea Institute of Science and Technology (KIST)
Jae-Yong Park: Institute of Health Science and Medical Research Center for Neural Dysfunction, Gyeongsang National University School of Medicine

Nature Communications, 2014, vol. 5, issue 1, 1-15

Abstract: 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.

Date: 2014
References: Add references at CitEc
Citations: View citations in EconPapers (1)

Downloads: (external link)
https://www.nature.com/articles/ncomms4227 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:5:y:2014:i:1:d:10.1038_ncomms4227

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/ncomms4227

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().