Abstract
Among ion channels, the K+-selective channels form the largest family and probably the most puzzling. Electrophysiological studies have revealed a wide variety of K+ currents which differ by their gating properties, their unitary conductance, their pharmacology and their regulations (RUDY 1988; HILLE 1992). A probable explanation for this diversity is to offer to each excitable cell the repertoire of K+ currents that is the most suitable for its function. Molecular characterization of K+ channels is recent. From the original cloning of the Shaker gene from the Drosophila in 1987, a deluge of data concerning the structure of K+ channels has occurred. Today, more than 100 pore-forming K+ channel subunits as well as a variety of auxiliary subunits have been cloned. Heterologous expression of these proteins has allowed to reconstitute voltage-gated (Kv), Ca2+-activated (KCa), inwardly rectifying (IRK), Gprotein-coupled (GIRK) and ATP-sensitive (KATP) K+ channels and to determine their biophysical, pharmacological, and regulation properties (for reviews see CHANDY et al. 1995; ROEPER et al. 1996; IsoMoTo et al. 1997; JAN et al. 1997; NICHOLS et al. 1997). On the other hand, the association of site-directed mutagenesis and electrophysiology techniques has allowed us to define structural features that are associated with particular K+ functional properties.
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Lesage, F., Lazdunski, M. (2000). Potassium Channels with Two Pore Domains. In: Endo, M., Kurachi, Y., Mishina, M. (eds) Pharmacology of Ionic Channel Function: Activators and Inhibitors. Handbook of Experimental Pharmacology, vol 147. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-57083-4_13
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DOI: https://doi.org/10.1007/978-3-642-57083-4_13
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