Article abstract


Nature Structural & Molecular Biology 15, 1152 - 1159 (2008)
Published online: 19 October 2008 | doi:10.1038/nsmb.1507

Activation of Slo1 BK channels by Mg2+ coordinated between the voltage sensor and RCK1 domains

Huanghe Yang1, Jingyi Shi1, Guohui Zhang1, Junqiu Yang1, Kelli Delaloye1 & Jianmin Cui1


The voltage-sensor domain (VSD) and the ligand sensor (cytoplasmic domain) of BK channels synergistically control channel activities, thereby integrating electrical and chemical signals for cell function. Studies show that intracellular Mg2+ mediates the interaction between these sensory domains to activate the channel through an electrostatic interaction with the VSD. Here we report that Mg2+ binds to a site that consists of amino acid side chains from both the VSD (Asp99 and Asn172) and the cytoplasmic domain (Glu374 and Glu399). For each Mg2+ binding site, the residues in the VSD and those in the cytoplasmic domain come from neighboring subunits. These results suggest that the VSD and the cytoplasmic domains from different subunits may interact during channel gating, and the packing of VSD or the RCK1 domain to the pore in BK channels differ from that in Kv1.2 or MthK channels.

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

Correspondence to: Jianmin Cui1 e-mail: jcui@biomed.wustl.edu



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