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Kv2.1 and electrically silent Kv6.1 potassium channel subunits combine and express a novel current
Author(s) -
Post Marc A.,
Kirsch Glenn E.,
Brown Arthur M.
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(96)01316-6
Subject(s) - xenopus , potassium channel , subfamily , biophysics , voltage clamp , protein subunit , patch clamp , voltage gated potassium channel , chemistry , microbiology and biotechnology , amino acid , biology , membrane potential , biochemistry , receptor , gene
Heteromultimer formation between Kv potassium channel subfamilies with the production of a novel current is reported for the first time. Protein‐protein interactions between Kv2.1 and electrically silent Kv6.1 α‐subunits were detected using two microelectrode voltage clamp and yeast two‐hybrid measurements. Amino terminal portions of Kv6.1 were unable to form homomultimers but interacted specifically with amino termini of Kv2.1. Xenopus oocytes co‐injected with Kv6.1 and Kv2.1 cRNAs exhibited a novel current with decreased rates of deactivation, decreased sensitivity to TEA block, and a hyperpolarizing shift of the half maximal activation potential when compared to Kv2.1. Our results indicate that Kv channel subfamilies can form heteromultimeric channels and, for the first time, suggest a possible functional role for the Kv6 subfamily.