My watch list
my.bionity.com  

my.bionity.com

With an accout for my.bionity.com you can always see everything at a glance – and you can configure your own website and individual newsletter.

  • My watch list
  • My saved searches
  • My saved topics
  • My newsletter
Register free of charge
Login  
eng  
DeutschEnglishFrançaisEspañol

BK channel



BK channels, also called Maxi-K or slo1 channels, are large conductance Ca2+ and voltage-activated K+ channels, which allow K+ to leave the cytoplasm under physiological conditions when activated by membrane potential and/or intracellular Ca2+ [4]. This results in hyperpolarization or a decrease in cell excitability. BK channels are essential for key physiological processes. They are important for controlling the contraction of smooth muscle and are also for electrical tuning of hair cells in the cochlea. BK channels are important for very high concentration (> 100 mM) behavioral effects of ethanol in the worm C. elegans [1]. It remains to be determined if, and how much, BK channels contribute to low intoxicating doses of ethanol (legal driving limit in most US states is 17.4 mM blood alcohol).

Structure

 

BK channels are a prime example of modular evolutionary protein design. The pore forming α-subunit consists of:

  1. The K+ permeable pore domain.
  2. The voltage sensing domain that are found in all other voltage gated K+ channels.
  3. A RCK domain that is involved in regulating the K+ conductance [3].
  4. A unique N-terminal transmembrane domain that is in addition to the usually 6 transmembrane domains in voltage dependent K+ channels.
  5. A unique large intracellular domain that acts as a sensor for the intracellular Ca2+ concentration [2].


References

  1. a  A central role of the BK potassium channel in behavioral responses to ethanol in C. elegans. Cell. 2003 Dec 12;115(6):655-66; PubMed
  2. a  A novel calcium-sensing domain in the BK channel. Biophys J. 1997 Sep;73(3):1355-63; PubMed Free text
  3. a  Structure of the RCK domain from the E. coli K+ channel and demonstration of its presence in the human BK channel. ; PubMed Free text
  4. a  An overview of the potassium channel family. Genome Biol. 2000; 1(4):reviews0004.1-0004.5; PubMed Free text

See also

v • d • e
Membrane transport protein: ion channels
Ca2+: Calcium channelVoltage-dependent calcium channel (L-type/Cavα(1.1, 1.2, 1.3, 1.4), N-type, P-type/Cavα(2.1), Q-type, R-type, T-type, β-subunits (β1, β2, β4), γ-subunits (γ2) • Inositol triphosphate receptor • Ryanodine receptor • Cation channels of sperm • Two-pore channel
Na+: Sodium channelNavα (1.1, 1.2, 1.4, 1.5, 1.7, 1.9) • Navβ (1, 3, 4) • Epithelial sodium channel
K+: Potassium channelVoltage-gated (Kvα (1.1, 1.2, 1.3, 1.4, 1.5, 2.1, 4.2, 4.3, 7.1, 7.2, 7.3, 7.4, 10.1, 11.1/hERG) • Kvβ (1, 2), Shaker gene, KCNE1) • Calcium-activated (BK channel, SK channel, SK3) • Inward-rectifier Kir (1.1, 2.1, 2.2, 2.3, 3.1, 3.2, 3.4, 4.1, 4.2, 6.1, 6.2)) • Tandem pore domain K2P (1, 2, 3, 4, 6, 9)
Cl-: Chloride channelCystic fibrosis transmembrane conductance regulator
PorinAquaporin (1, 2, 3, 4) • Voltage-dependent anion channel (1)
Cations: TRPTRPA (1) • TRPC (1, 2, 3, 4, 4AP, 5, 6, 7) • TRPM (1, 2, 3, 4, 5, 6, 7, 8) • TRPML (Mucolipin-1) • TRPP (1, 2)• TRPV (1, 2, 3, 4, 5, 6)
Other/generalVoltage-gated ion channel • Ligand-gated ion channel • Cyclic nucleotide-gated ion channel (α1, α3, β3, H1, H2, H4) • Stretch-activated ion channel
 
This article is licensed under the GNU Free Documentation License. It uses material from the Wikipedia article "BK_channel". A list of authors is available in Wikipedia.
Your browser is not current. Microsoft Internet Explorer 6.0 does not support some functions on Chemie.DE