Transmembrane movement of the Shaker K+ channel S4

H. Peter Larsson, Oliver S. Baker, Dalvinder S. Dhillon, Ehud Y. Isacoff

Research output: Contribution to journalArticlepeer-review

445 Scopus citations


We have probed internal and external accessibility of S4 residues to the membrane-impermeant thiol reagent methanethiosulfonate- ethyltrimethylammonium (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.

Original languageEnglish (US)
Pages (from-to)387-397
Number of pages11
Issue number2
StatePublished - Feb 1996
Externally publishedYes

ASJC Scopus subject areas

  • Neuroscience(all)


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