Cellular and Molecular Life Sciences

, Volume 66, Issue 5, pp 852–875

Molecular mechanisms of BK channel activation

Review

DOI: 10.1007/s00018-008-8609-x

Cite this article as:
Cui, J., Yang, H. & Lee, U.S. Cell. Mol. Life Sci. (2009) 66: 852. doi:10.1007/s00018-008-8609-x

Abstract.

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.

Keywords.

Channel gatingMaxiKcalcium activationvoltage activationmetal bindingallosteric

Copyright information

© Birkhäuser Verlag, Basel 2008

Authors and Affiliations

  1. 1.Department of Biomedical Engineering and Cardiac Bioelectricity and Arrhythmia CenterWashington UniversitySt. LouisUSA