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XB-ART-20555
J Physiol 1994 Nov 15;481 ( Pt 1):7-13.
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Reversal of rectification and alteration of selectivity and pharmacology in a mammalian Kv1.1 potassium channel by deletion of domains S1 to S4.

Tytgat J , Vereecke J , Carmeliet E .


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1. A possible relation between the family of inwardly rectifying K+ channels and the Shaker superfamily of K+ channels was investigated using a deletion mutant (DelS1-S4) of a delayed rectifier Kv1.1 (RCK1) K+ channel. 2. The mutant DelS1-S4 was made by eliminating the sequence coding for transmembrane domains S1 to S4 of the Kv1.1 K+ channel, and re-ligating the sequence coding for the cytoplasmic amino terminus to transmembrane domain S5. Microelectrode voltage-clamp and patch-clamp experiments were performed on Xenopus laevis oocytes after injection of in vitro transcribed mRNA coding for mutant and wild-type channels. 3. The lack of transmembrane domains S1 to S4 converts a depolarization-activated wild-type Kv1.1 K+ channel with outward rectification into a hyperpolarization-activated channel with inward rectification. Although the pore region of the deletion mutant is identical to the wild-type channel, the mutant channel is a non-selective cation channel and is characterized by an altered pharmacology profile.

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Species referenced: Xenopus laevis
Genes referenced: kcna1

References [+] :
Babila, Assembly of mammalian voltage-gated potassium channels: evidence for an important role of the first transmembrane segment. 1994, Pubmed, Xenbase