KCNKØ: Opening and closing the 2-P-domain potassium leak channel entails "C-type" gating of the outer pore

Noam Zilberberg, Nitza Ilan, Steve A.N. Goldstein

Research output: Contribution to journalArticlepeer-review

76 Scopus citations

Abstract

Essential to nerve and muscle function, little is known about how potassium leak channels operate. KCNKØ opens and closes in a kinase-dependent fashion. Here, the transition is shown to correspond to changes in the outer aspect of the ion conduction pore. Voltage-gated potassium (VGK) channels open and close via an internal gate; however, they also have an outer pore gate that produces "C-type" inactivation. While KCNKØ does not inactivate, KCNKØ and VGK channels respond in like manner to outer pore blockers, potassium, mutations, and chemical modifiers. Structural relatedness is confirmed: VGK residues that come close during C-type gating predict KCNKØ sites that crosslink (after mutation to cysteine) to yield channels controlled by reduction and oxidization. We conclude that similar outer pore gates mediate KCNKØ opening and closing and VGK channel C-type inactivation despite their divergent structures and physiological roles.

Original languageEnglish
Pages (from-to)635-648
Number of pages14
JournalNeuron
Volume32
Issue number4
DOIs
StatePublished - 20 Nov 2001
Externally publishedYes

ASJC Scopus subject areas

  • General Neuroscience

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