A conserved glutamate is important for slow inactivation in K+ channels

Hans P Larsson, Fredrik Elinder

Research output: Contribution to journalArticle

80 Scopus citations

Abstract

Voltage-gated ion channels undergo slow inactivation during prolonged depolarizations. We investigated the role of a conserved glutamate at the extracellular end of segment 5 (S5) in slow inactivation by mutating it to a cysteine (E418C in Shaker). We could lock the channel in two different conformations by disulfidelinking 418C to two different cysteines, introduced in the Pore-S6(P-S6) loop. Our results suggest that E418 is normally stabilizing the open conformation of the slow inactivation gate by forming hydrogen bonds with the P-S6 loop. Breaking these bonds allows the P-S6 loop to rotate, which closes the slow inactivation gate. Our results also suggest a mechanism of how the movement of the voltage sensor can induce slow inactivation by destabilizing these bonds.

Original languageEnglish
Pages (from-to)573-583
Number of pages11
JournalNeuron
Volume27
Issue number3
StatePublished - Dec 7 2000
Externally publishedYes

    Fingerprint

ASJC Scopus subject areas

  • Neuroscience(all)

Cite this