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Vol. 273, Issue 2, 681-684, January 9, 1998
From the Howard Hughes Medical Institute, Departments of Internal
Medicine and Physiology and Biophysics, University of Iowa College of
Medicine, Iowa City, Iowa 52242
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 (
, 
, and 
) with
subunits containing mutations that alter channel inhibition by
methanethiosulfonates. The data indicate that hENaC contains three ,
three , and three subunits. Sucrose gradient sedimentation of
hENaC translated in vitro, as well as -, -, and
hENaC 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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