Abstract
Voltage-dependent movement of a sodium channel S4 segment was examined by cysteine scanning mutagenesis and testing accessibility of the residues to hydrophilic cysteine-modifying reagents. These experiments indicate that 2 charged S4 residues move completely from an internally accessible to an externally accessible location in response to depolarization by passage through a short 'channel' in the protein. The energetic problems of S4 movement have thus been solved in the same way that many ion channels achieve highly selective and rapid ion permeation through an open pore, by restricting the contact region between the permion and its channel.
Original language | English (US) |
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Pages (from-to) | 113-122 |
Number of pages | 10 |
Journal | Neuron |
Volume | 16 |
Issue number | 1 |
DOIs | |
State | Published - Jan 1996 |
Funding
We thank Drs. Michael O'Leary and Carol Deutsch for helpful discussions and comments on the manuscript, Dr. Fred Sigworth for insightful discussions, and Aaron Benson and Vincent Santarelli for technical assistance with mutagenesis and tissue culture. Supported by National Institutes of Health grants AR41691 (R. H.) and NS32387 (A. L. G.). A. L. G. is a Lucille P. Markey Scholar.
ASJC Scopus subject areas
- General Neuroscience