Journal article
Specificity of charge-carrying residues in the voltage sensor of potassium channels
The Journal of general physiology, Vol.123(3), pp.205-216
03/2004
DOI: 10.1085/jgp.200308993
PMCID: PMC2217452
PMID: 14769847
Abstract
Positively charged voltage sensors of sodium and potassium channels are driven outward through the membrane's electric field upon depolarization. This movement is coupled to channel opening. A recent model based on studies of the KvAP channel proposes that the positively charged voltage sensor, christened the "voltage-sensor paddle", is a peripheral domain that shuttles its charged cargo through membrane lipid like a hydrophobic cation. We tested this idea by attaching charged adducts to cysteines introduced into the putative voltage-sensor paddle of Shaker potassium channels and measuring fractional changes in the total gating charge from gating currents. The only residues capable of translocating attached charges through the membrane-electric field are those that serve this function in the native channel. This remarkable specificity indicates that charge movement involves highly specialized interactions between the voltage sensor and other regions of the protein, a mechanism inconsistent with the paddle model.
Details
- Title: Subtitle
- Specificity of charge-carrying residues in the voltage sensor of potassium channels
- Creators
- Christopher A Ahern - Department of Physiology, Jefferson Medical College, 1020 Locust Street, Philadelphia, PA 19107, USARichard Horn
- Resource Type
- Journal article
- Publication Details
- The Journal of general physiology, Vol.123(3), pp.205-216
- DOI
- 10.1085/jgp.200308993
- PMID
- 14769847
- PMCID
- PMC2217452
- NLM abbreviation
- J Gen Physiol
- ISSN
- 0022-1295
- eISSN
- 1540-7748
- Publisher
- United States
- Grant note
- R01 AR041691 / NIAMS NIH HHS AR41691 / NIAMS NIH HHS
- Language
- English
- Date published
- 03/2004
- Academic Unit
- Molecular Physiology and Biophysics; Iowa Neuroscience Institute
- Record Identifier
- 9984070159302771
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