mechano-gated K₂P channel TREK-1

• Published in: European biophysics journal Vol. 38; no. 3; pp. 293 - 303
• Main Authors: Dedman, Alexandra, Sharif-Naeini, Reza, Folgering, Joost H. A, Duprat, Fabrice, Patel, Amanda, Honoré, Eric
• Format: Journal Article
• Language: English
• Published: Berlin/Heidelberg Berlin/Heidelberg : Springer-Verlag 2009; Springer-Verlag; Springer Nature B.V
• Subjects: Biochemistry; Biological and Medical Physics; Biomedical and Life Sciences; Biophysics; Cell Biology; Genes; Ions; Life Sciences; Membrane Biology; Nanotechnology; Neurobiology; Neurons; Pharmacology; Physiology; Potassium; Review; Stretch; Ion channels; Mechanotransduction; Pharmacology; Physiology; Potassium
• ISSN: 0175-7571; 1432-1017
• DOI: 10.1007/s00249-008-0318-8

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 (K₂P) make up one class of K⁺ channels along with the inward rectifiers and the voltage- and/or calcium-dependent K⁺ channels. Each K₂P 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 K₂P channel TREK-1 and will emphasize on the polymodal function of this “unconventional” K⁺ channel.