Na+ Interaction with the Pore of Shaker B K+ Channels

Abstract

The Shaker B K+ conductance (GK) collapses (in a reversible manner) if the membrane is depolarized and then repolarized in, 0 K+, Na+-containing solutions (Gómez-Lagunas, F. 1997. J. Physiol. 499:3–15; Gómez-Lagunas, F. 1999. Biophys. J. 77:2988–2998). In this work, the role of Na+ ions in the collapse of GK in 0-K+ solutions, and in the behavior of the channels in low K+, was studied. The main findings are as follows. First, in 0-K+ solutions, the presence of Na+ ions is an important factor that speeds the collapse of GK. Second, external Na+ fosters the drop of GK by binding to a site with a Kd = 3.3 mM. External K+ competes, in a mutually exclusive manner, with Nao+ for binding to this site, with an estimated Kd = 80 μM. Third, NMG and choline are relatively inert regarding the stability of GK; fourth, with [Ko+] = 0, the energy required to relieve Nai+ block of Shaker (French, R.J., and J.B. Wells. 1977. J. Gen. Physiol. 70:707–724; Starkus, J.G., L. Kuschel, M. Rayner, and S. Heinemann. 2000. J. Gen. Physiol. 110:539–550) decreases with the molar fraction of Nai+ (XNa,i), in an extent not accounted for by the change in ΔμNa. Finally, when XNa,i = 1, GK collapses by the binding of Nai+ to two sites, with apparent Kds of 2 and 14.3 mM.