Key result
External barium interacts with the permeation pathway of KCNQ1 at two discrete sites, causing voltage-dependent pore blockade and unique gating alterations.
External barium interacts with KCNQ1 channels at two distinct sites, highlighting significant structural and functional uniqueness in its pore region compared to other K+ channels.
Barium's dual-site KCNQ1 blockade in animal models warrants no clinical inference; leaves open pore uniqueness versus other K+ channels for human validation.
The pore properties and the reciprocal interactions between permeant ions and the gating of KCNQ channels are poorly understood. Here we used external barium to investigate the permeation characteristics of homomeric KCNQ1 channels. We assessed the Ba(2+) binding kinetics and the concentration and voltage dependence of Ba(2+) steady-state block. Our results indicate that extracellular Ba(2+) exerts a series of complex effects, including a voltage-dependent pore blockade as well as unique gating alterations. External barium interacts with the permeation pathway of KCNQ1 at two discrete and nonsequential sites. (a) A slow deep Ba(2+) site that occludes the channel pore and could be simulated by a model of voltage-dependent block. (b) A fast superficial Ba(2+) site that barely contributes to channel block and mostly affects channel gating by shifting rightward the voltage dependence of activation, slowing activation, speeding up deactivation kinetics, and inhibiting channel inactivation. A model of voltage-dependent block cannot predict the complex impact of Ba(2+) on channel gating in low external K(+) solutions. Ba(2+) binding to this superficial site likely modifies the gating transitions states of KCNQ1. Both sites appear to reside in the permeation pathway as high external K(+) attenuates Ba(2+) inhibition of channel conductance and abolishes its impact on channel gating. Our data suggest that despite the high degree of homology of the pore region among the various K(+) channels, KCNQ1 channels display significant structural and functional uniqueness.
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Gibor et al. (2004) studied KCNQ1 potassium channels. External barium was evaluated on Ba(2+) binding kinetics and steady-state block. External barium interacts with the permeation pathway of KCNQ1 at two discrete sites, causing voltage-dependent pore blockade and unique gating alterations.
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