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Updated: Aug 4, 2026

Mutagenesis and Functional Analysis of Ion Channels Heterologously Expressed in Mammalian Cells
Published on: October 1, 2010
Mutants of a temperature-sensitive two-P domain potassium channel
M T Kunkel1, D B Johnstone, J H Thomas
1Departments of Anatomy, Washington University School of Medicine, Seattle, Washington, USA.
Abstract:
Within the Caenorhabditis elegans genome there exist at least 42 genes encoding TWK (two-P domain K(+)) channels, potassium channel subunits that contain two pore regions and four transmembrane domains. We now report the first functional characterization of a TWK channel from C. elegans. Although potassium channels have been reported to be activated by a variety of factors, TWK-18 currents increase dramatically with increases in temperature. Two mutant alleles of the twk-18 gene confer uncoordinated movement and paralysis in C. elegans. Expression of wild-type and mutant TWK-18 channels in Xenopus oocytes showed that mutant channels express much larger potassium currents than wild-type channels. Promoter-green fluorescent protein fusion experiments indicate that TWK-18 is expressed in body wall muscle. Our genetic and physiological data suggest that the movement defects observed in mutant twk-18 animals may be explained by an increased activity of the mutant TWK-18 channels.
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