Cloning and functional characterization of the smooth muscle ether-a-go-go-related gene K+ channel. Potential role of a conserved amino acid substitution in the S4 region - PubMed (original) (raw)
. 2003 Jan 24;278(4):2503-14.
doi: 10.1074/jbc.M208525200. Epub 2002 Nov 9.
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- PMID: 12427763
- DOI: 10.1074/jbc.M208525200
Free article
Cloning and functional characterization of the smooth muscle ether-a-go-go-related gene K+ channel. Potential role of a conserved amino acid substitution in the S4 region
Fouzia Shoeb et al. J Biol Chem. 2003.
Free article
Erratum in
- J Biol Chem. 2004 Nov 12;279(46):48486
Abstract
The human ether-a-go-go-related gene (HERG) product forms the pore-forming subunit of the delayed rectifier K(+) channel in the heart. Unlike the cardiac isoform, the erg K(+) channels in native smooth muscle demonstrate gating properties consistent with a role in maintaining resting potential. We have cloned the smooth muscle isoform of HERG, denoted as erg1-sm, from human and rabbit colon. erg1-sm is truncated by 101 amino acids in the C terminus due to a single nucleotide deletion in the 14th exon. Sequence alignment against HERG showed a substitution of alanine for valine in the S4 domain. When expressed in Xenopus oocytes, erg1-sm currents had much faster activation and deactivation kinetics compared with HERG. Step depolarization positive to -20 mV consistently produced a transient outward component. The threshold for activation of erg1-sm was -60 mV and steady-state conductance was approximately 10-fold greater than HERG near the resting potential of smooth muscle. Site-directed mutagenesis of alanine to valine in the S4 region of erg1-sm converted many of the properties to that of the cardiac HERG, including shifts in the voltage dependence of activation and slowing of deactivation. These studies define the functional role of a novel isoform of the ether-a-go-go-related gene K(+) channel in smooth muscle.
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