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pubmed-article:1419000pubmed:abstractTextThe 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.lld:pubmed
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pubmed-article:1419000pubmed:articleTitleSubunit stoichiometry of a mammalian K+ channel determined by construction of multimeric cDNAs.lld:pubmed
pubmed-article:1419000pubmed:affiliationDepartment of Cellular and Molecular Physiology, Harvard Medical School, Boston, Massachusetts 02115.lld:pubmed
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pubmed-article:1419000pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
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