Electrophysiological and biochemical evidence that DEG/ENaC cation channels are composed of nine subunits

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Abstract

Members of the DEG/ENaC protein family form ion channels with diverse functions. DEG/ENaC subunits associate as hetero- and homomultimers to generate channels; however the stoichiometry of these complexes is unknown. To determine the subunit stoichiometry of the human epithelial Na+ channel (hENaC), we expressed the three wild-type hENaC subunits (α, β, and γ) with subunits containing mutations that alter channel inhibition by methanethiosulfonates. The data indicate that hENaC contains three α, three β, and three γ subunits. Sucrose gradient sedimentation of αhENaC translated in vitro, as well as α-, β-, and γhENaC coexpressed in cells, was consistent with complexes containing nine subunits. FaNaCh and BNC1, two related DEG/ENaC channels, produced complexes of similar mass. Our results suggest a novel nine-subunit stoichiometry for the DEG/ENaC family of ion channels.

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Snyder, P. M., Cheng, C., Prince, L. S., Rogers, J. C., & Welsh, M. J. (1998). Electrophysiological and biochemical evidence that DEG/ENaC cation channels are composed of nine subunits. Journal of Biological Chemistry, 273(2), 681–684. https://doi.org/10.1074/jbc.273.2.681

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