Co-expression of Kv6.1 and Kv2.1 in Xenopus oocytes produced a novel current with decreased deactivation rates, decreased TEA block sensitivity, and a hyperpolarizing shift in activation potential.
Does co-expression of Kv6.1 and Kv2.1 produce a novel potassium current in Xenopus oocytes?
This study provides the first evidence that Kv channel subfamilies can form heteromultimeric channels, suggesting a functional role for the electrically silent Kv6 subfamily.
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 alpha-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.
Post et al. (Mon,) reported a other. Co-injection of Kv6.1 and Kv2.1 cRNAs vs. Kv2.1 alone was evaluated on Current characteristics (deactivation rate, TEA block sensitivity, half maximal activation potential). Co-expression of Kv6.1 and Kv2.1 in Xenopus oocytes produced a novel current with decreased deactivation rates, decreased TEA block sensitivity, and a hyperpolarizing shift in activation potential.
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