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Abstract
The subunit stoichiometry of the mammalian K+ channel KV1.1 (RCK1) was examined by
linking together the coding sequences of 2-5 K+ channel subunits in a single open
reading frame and tagging the expression of individual subunits with a mutation (Y379K
or Y379R) that altered the sensitivity of the channel to block by external tetraethylammonium
ion. Two lines of evidence argue that these constructs lead to K+ channel expression
only through the formation of functional tetramers. First, currents expressed by tetrameric
constructs containing a single mutant subunit have a sensitivity to tetraethylammonium
that is well fitted by a single site binding isotherm. Second, a mutant subunit (Y379K)
that expresses only as part of a heteromultimer contributes to the expression of functional
channels when coexpressed with a trimeric construct but not a tetrameric construct.