Multiple subunits of a voltage-dependent potassium channel contribute to the binding site for tetraethylammonium

M. P. Kavanaugh, R. S. Hurst, J. Yakel, M. D. Varnum, J. P. Adelman, R. A. North

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Abstract

RNAs encoding a wild-type (RBK1) and a mutant (RBK1(Y379V,V381 T); RBK1*) subunit of voltage-dependent potassium channels were injected into Xenopus oocytes. When expressed separately, they made homotetrameric channels that differed about 100-fold in sensitivity to tetraethylammonium (TEA). Mixtures of channels having one, two, or three low affinity subunits were expressed by injecting various proportions of RBK1 and RBK1* RNAs. The affinity for TEA of these three channel species was deduced by fitting concentration-response curves for the inhibition of potassium currents. DNAs were also concatenated to construct a sequence that encoded two connected subunits, and channels that contained four, two, or no TEA-sensitive subunits were expressed. The results suggest that bound TEA interacts simultaneously with all four subunits.

Original languageEnglish (US)
Pages (from-to)493-497
Number of pages5
JournalNeuron
Volume8
Issue number3
DOIs
StatePublished - Mar 1992

ASJC Scopus subject areas

  • Neuroscience(all)

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    Kavanaugh, M. P., Hurst, R. S., Yakel, J., Varnum, M. D., Adelman, J. P., & North, R. A. (1992). Multiple subunits of a voltage-dependent potassium channel contribute to the binding site for tetraethylammonium. Neuron, 8(3), 493-497. https://doi.org/10.1016/0896-6273(92)90277-K