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Article

The contribution of individual subunits to the coupling of the voltage sensor to pore opening in Shaker K channels: effect of ILT mutations in heterotetramers.

The Journal of general physiology - 1 Nov 2010

Gagnon Dominique G, Bezanilla Francisco

Abstract excerpt

Voltage-gated ion channels couple conformational change(s) of the voltage-sensing domain to those of the opening of an intracellular gate to allow ionic conduction. Much larger positive potentials are required to couple these conformational changes to the opening of the gate of Shaker K(+) channe...

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Identifiers

PMID: 20974773
DOI: 10.1085/jgp.201010487
PMCID: PMC2964516

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-20974773-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

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The contribution of individual subunits to the coupling of the voltage sensor to pore opening in Shaker K channels: effect of ILT mutations in heterotetramers.PMID 20974773Read ↗

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Mutations in the S6 gate isolate a late step in the activation pathway and reduce 4-AP sensitivity in shaker K(v) channel.Semantic proximity Read ↗

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A characterization of the activating structural rearrangements in voltage-dependent Shaker K+ channels.Semantic proximity Read ↗

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Functional interactions at the interface between voltage-sensing and pore domains in the Shaker K(v) channel.Semantic proximity Read ↗

Gating interaction maps reveal a noncanonical electromechanical coupling mode in the Shaker K+ channel.Semantic proximity Read ↗

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