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pubmed-article:8789953pubmed:abstractTextWe have probed internal and external accessibility of S4 residues to the membrane-impermeant thiol reagent methanethiosulfonate-ethyltrimethlammonium (MTSET) in both open and closed, cysteine-substituted Shaker K+ channels. Our results indicate that S4 traverses the membrane with no more than 5 amino acids in the closed state, and that the distribution of buried residues changes when channels open. This change argues for a displacement of S4 through the plane of the membrane in which an initially intracellular residue moves to within 3 amino acids of the extracellular solution. These results demonstrate that the putative voltage-sensing charges of S4 actually reside in the membrane and that they move outward when channels open. We consider constraints placed on channel structure by these results.lld:pubmed
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pubmed-article:8789953pubmed:articleTitleTransmembrane movement of the shaker K+ channel S4.lld:pubmed
pubmed-article:8789953pubmed:affiliationDepartment of Molecular and Cell Biology, University of California, Berkeley 94720, USA.lld:pubmed
pubmed-article:8789953pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:8789953pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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