Dissecting the coupling between the voltage sensor and pore domains.
The gating mechanism of K(v) channels is not known. In this issue of Neuron, Soler-Llavina et al. present fascinating results that support the concept of relatively independent voltage-sensing modules. However, they also find that its interactions with the pore domain are rather complex, with specific S4-S5 intersubunit contacts underlying the concerted transition leading to the channel opening.
Roux
Benoit
B
Institute for Molecular Pediatric Sciences and Department of Biochemistry and Molecular Biology, University of Chicago, Gordon Center for Integrative Sciences, 929 East 57th Street, Chicago, Ilinois 60637, USA.
D000818:Animals; D002462:Cell Membrane / Q000378:metabolism*; D018360:Crystallography, X-Ray; D006801:Humans; D015640:Ion Channel Gating / Q000502:physiology*; D051663:Kv1.2 Potassium Channel / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D008564:Membrane Potentials / Q000502:physiology; D024642:Potassium Channels, Voltage-Gated / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D017434:Protein Structure, Tertiary / Q000502:physiology; D021122:Protein Subunits / Q000737:chemistry / Q000378:metabolism
D051663:Kv1.2 Potassium Channel; D024642:Potassium Channels, Voltage-Gated; D021122:Protein Subunits