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Cell Mol Life Sci. 2009 Mar;66(5):852-75. doi: 10.1007/s00018-008-8609-x.

Molecular mechanisms of BK channel activation.

Author information

1
Department of Biomedical Engineering and Cardiac Bioelectricity and Arrhythmia Center, Washington University, 1 Brookings Drive, St. Louis, Missouri 63130, USA. jcui@biomed.wustl.edu

Abstract

Large conductance, Ca(2+)-activated potassium (BK) channels are widely expressed throughout the animal kingdom and play important roles in many physiological processes, such as muscle contraction, neural transmission and hearing. These physiological roles derive from the ability of BK channels to be synergistically activated by membrane voltage, intracellular Ca(2+) and other ligands. Similar to voltage-gated K(+) channels, BK channels possess a pore-gate domain (S5-S6 transmembrane segments) and a voltage-sensor domain (S1-S4). In addition, BK channels contain a large cytoplasmic C-terminal domain that serves as the primary ligand sensor. The voltage sensor and the ligand sensor allosterically control K(+) flux through the pore-gate domain in response to various stimuli, thereby linking cellular metabolism and membrane excitability. This review summarizes the current understanding of these structural domains and their mutual interactions in voltage-, Ca(2+)- and Mg(2+)-dependent activation of the channel.

PMID:
19099186
PMCID:
PMC2694844
DOI:
10.1007/s00018-008-8609-x
[Indexed for MEDLINE]
Free PMC Article

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