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The mechano-gated K(2P) channel TREK-1.

Authors
  • Dedman, Alexandra
  • Sharif-Naeini, Reza
  • Folgering, Joost H A
  • Duprat, Fabrice
  • Patel, Amanda
  • Honoré, Eric
Type
Published Article
Journal
European Biophysics Journal
Publisher
Springer-Verlag
Publication Date
Mar 01, 2009
Volume
38
Issue
3
Pages
293–303
Identifiers
DOI: 10.1007/s00249-008-0318-8
PMID: 18369610
Source
Medline
License
Unknown

Abstract

The versatility of neuronal electrical activity is largely conditioned by the expression of different structural and functional classes of K+ channels. More than 80 genes encoding the main K+ channel alpha subunits have been identified in the human genome. Alternative splicing, heteromultimeric assembly, post-translational modification and interaction with auxiliary regulatory subunits further increase the molecular and functional diversity of K+ channels. Mammalian two-pore domain K+ channels (K(2P)) make up one class of K+ channels along with the inward rectifiers and the voltage- and/or calcium-dependent K+ channels. Each K(2P) channel subunit is made up of four transmembrane segments and two pore-forming (P) domains, which are arranged in tandem and function as either homo- or heterodimeric channels. This novel structural arrangement is associated with unusual gating properties including "background" or "leak" K+ channel activity, in which the channels show constitutive activity at rest. In this review article, we will focus on the lipid-sensitive mechano-gated K(2P) channel TREK-1 and will emphasize on the polymodal function of this "unconventional" K+ channel.

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