Molecular mechanisms of BK channel activation.
Molecular mechanisms of BK channel activation.
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DOI：
10.1007/s00018-008-8609-x
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发表时间：
2009-03
影响因子：
8
通讯作者：
Lee, U. S.
中科院分区：
文献类型：
--
作者：
Cui, J.;Yang, H.;Lee, U. S.
Large conductance, Ca2+-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 Ca2+ 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-, Ca2+- and Mg2+-dependent activation of the channel.
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DOI：
10.1085/jgp.105.1.49
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