Potassium Channels

Potassium channels constitute a highly diverse class of ion channel and thus participate in multiple modulatory functions. There are several functional types of K+ channel, including voltage-gated K+ channels, Ca2+-activated K+ channels, inward rectifiers, leak K+ channels and Na+-activated K+ channels. Principal or pore-forming subunits of at least the first four types have been identified and are classified into three groups of proteins on the basis of their structural properties.

Keywords: potassium channels; ion channels; electrophysiology; membrane proteins; transport proteins

Figure 1. Functional K+ channels in mammalian cells can be divided into those that are activated by Ca2+ (Ca2+-activated K+ channels) or membrane voltage (voltage-activated K+ channels). The K+ channels not gated by voltage either exhibit the property of inward rectification (inward rectifier K+ channels) or behave as simple K+-permeable ‘holes’ in the membrane (‘leak’ K+ channels). Na+-activated K+ channels are not shown here.
Figure 2. Classification of K+ channel principal subunits into those having two, four or six transmembrane domains (TMDs) in a continuous polypeptide. Transmembrane segments are shown as cylinders spanning the membrane (the intra- and extracellular side is indicated). The schematic views from the top illustrate the dimeric (in the case of four-TMD channels) or tetrameric (in the case of two-TMD or six-TMD channels structure). The darker shading represents one of the principal subunits in the channel complex.
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 References
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 Further Reading
    Abbott GW and Goldstein SA (1998) A superfamily of small potassium channel subunits: form and function of the MinK-related peptides (MiRPs). Quarterly Review of Biophysics 31: 357–398.
    book Ashcroft FM (2000) Ion Channels and Disease. New York, NY: Academic Press.
    Bauer CK and Schwarz JR (2001) Physiology of eag K+ channels. Journal of Membrane Biology 182: 1–15.
    Goldstein SA, Bockenhauer D, O'Kelly I and Zilberberg N (2001) Potassium leak channels and the KCNK family of two-P-domain subunits. Nature Reviews Neuroscience 2: 175–184.
    Jan LY and Jan YN (1997) Cloned potassium channels from eukaryotes and prokaryotes. Annual Review of Neuroscience 20: 91–123.
    book Kurachi Y, Jan LY and Lazdunski M (1999) Potassium Ion Channels. Molecular Structure, Function and Diseases. San Diego, CA: Academic Press.
    Patel AJ and Honore E (2001) Molecular physiology of oxygen-sensitive potassium channels. European Respiratory Journal: Official Journal of the European Society for Clinical Respiratory Physiology 18: 221–227.
    Rudy B and McBain CJ (2001) Kv3 channels: voltage-gated K+ channels designed for high-frequency repetitive firing. Trends in Neurosciences 24: 517–526.
    book Rudy B and Seeburg P (1999) Molecular and Functional Diversity of Ion Channels and Receptors. New York, NY: New York Academy of Sciences.
    Vergara C, Latorre R, Marrion NV and Adelman JP (1998) Calcium-activated potassium channels. Current Opinion in Neurobiology 8: 321–329.
 Web Links
    ePath Molecular Diversity of K+ Channels http://k-channels.med.nyu.edu/
    ePath Mammalian 2P domain and background K+ channels (K2P) http://www.ipmc.cnrs.fr/~duprat/2p/index.htm
    ePath Permeation of Ions Across the Potassium Channel http://anusf.anu.edu.au/Vizlab/viz_showcase/shinho_chung/
    ePath Ion Channels, Transmitters, Receptors and Disease http://www.neuro.wustl.edu/neuromuscular/mother/chan.html
    ePath Neurotoxins http://faculty.washington.edu/chudler/toxin1.html
    ePath Ion Channel Slides http://www.sigma-aldrich.com/saws.nsf/Pages/sg_ls_cs_ionchannelslide_home
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Coetzee, William A, and Rudy, Bernardo(Jan 2006) Potassium Channels. In: eLS. John Wiley & Sons Ltd, Chichester. http://www.els.net [doi: 10.1038/npg.els.0005670]