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- W2041782951 abstract "In voltage- and ligand-gated ion channels the voltage sensor domain (VSD) and the ligand sensor change conformation upon stimulation, which then triggers the activation gate to open. However, the retrograde control of the conformation of the sensors by the activation gate has not been well studied. Recently, we reported that Mg2+ binds to the interface between the cytosolic domain and the membrane-spanning VSD of BK type Ca2+-activated K+ channels and activates the voltage sensor through an electrostatic interaction (Yang et al., 2007; Yang et al., 2008). Here we show that the interaction between Mg2+ and the voltage sensor is controlled by the opening of the activation gate. A mutation (F315A) in the middle of the pore-lining S6 segment altered channel opening such that the channels did not open even though the voltage sensor was fully active. The lock of the channel at the closed conformation also abolished the electrostatic interaction between Mg2+ and the VSD. 100 μm [Ca2+]i opened the activation gate of the mutant channel and reestablished the electrostatic interaction. Therefore, the activation gate and the sensory domains in BK channels are allosterically coupled and undergo concerted movements during channel gating. References: Yang, H. et al. 2007. Proc. Natl. Acad. Sci. U. S. A. 104:18270-18275. Yang, H. et al. 2008. Nat. Struct. Mol. Biol. (In press)." @default.
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- W2041782951 date "2009-02-01" @default.
- W2041782951 modified "2023-10-18" @default.
- W2041782951 title "Gate Opening Remotely Controls the Interaction between the Voltage Sensor and the Cytosolic Domain in BK Channels" @default.
- W2041782951 doi "https://doi.org/10.1016/j.bpj.2008.12.2479" @default.
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