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BK channels, also called MaxiK 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 voltage and/or intracellular Ca2+ . 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 . 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[edit | edit source]
BK channels are a prime example of modular evolutionary protein design. The pore forming α-subunit consists of:
- The K+ permeable pore domain.
- The voltage sensing domain that are found in all other voltage gated K+ channels.
- A RCK domain that is involved in regulating the K+ conductance .
- A unique N-terminal transmembrane domain that is in addition to the usually 6 transmembrane domains in voltage dependent K+ channels.
- A unique large intracellular domain that acts as a sensor for the intracellular Ca2+ concentration .
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References[edit | edit source]
A central role of the BK potassium channel in behavioral responses to ethanol in C. elegans. Cell. 2003 Dec 12;115(6):655-66; PMID 14675531
A novel calcium-sensing domain in the BK channel. Biophys J. 1997 Sep;73(3):1355-63; PMID 9284303 Free text
Structure of the RCK domain from the E. coli K+ channel and demonstration of its presence in the human BK channel. ; PMID 11301020 Free text
An overview of the potassium channel family. Genome Biol. 2000; 1(4):reviews0004.1-0004.5; PMID 11178249 Free text
See also[edit | edit source]
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