Evidence for lateral mobility of voltage sensors in prokaryotic voltage-gated sodium channels

Biochemical and Biophysical Research Communications
Hitoshi NaguraYoshinori Fujiyoshi

Abstract

Voltage-sensor domains (VSDs) in voltage-gated ion channels are thought to regulate the probability that a channel adopts an open conformation by moving vertically in the lipid bilayer. Here we characterized the movement of the VSDs of the prokaryotic voltage-gated sodium channel, NaChBac. Substitution of residue T110, which is located on the extracellular side of the fourth transmembrane helix of the VSD, by cysteine resulted in the formation of a disulfide bond between adjacent subunits in the channel. Our results suggest that T110 residues in VSDs of adjacent subunits can come into close proximity, implying that the VSDs can move laterally in the membrane and constitute a mechanism that regulates channel activity.

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Citations

Dec 24, 2010·The Journal of Biological Chemistry·Takushi ShimomuraYoshinori Fujiyoshi
Mar 19, 2011·Protein Science : a Publication of the Protein Society·Yoshinori Fujiyoshi
Feb 13, 2013·Proceedings of the National Academy of Sciences of the United States of America·Liang ShiQiu-Xing Jiang

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