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Article

Lack of negatively charged residues at the external mouth of Kir2.2 channels enable the voltage-dependent block by external Mg2+.

PloS one - 1 Jan 2014

Li Junwei, Xie Xiaoxiao, Liu Jun, Yu Hui, Zhang Suhua, Zhan Yong, Zhang Hailin, Logothetis Diomedes E, An Hailong

Abstract excerpt

Kir channels display voltage-dependent block by cytosolic cations such as Mg2+ and polyamines that causes inward rectification. In fact, cations can regulate K channel activity from both the extracellular and intracellular sides. Previous studies have provided insight into the up-regulation of Kir channel activity by extracellular K+ concentration. In contrast, extracellular Mg2+ has been found to reduce the...

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Identifiers

PMID: 25350118
DOI: 10.1371/journal.pone.0111372
PMCID: PMC4211740

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Lack of negatively charged residues at the external mouth of Kir2.2 channels enable the voltage-dependent block by external Mg2+.PMID 25350118Read ↗

Identification of a site involved in the block by extracellular Mg(2+) and Ba(2+) as well as permeation of K(+) in the Kir2.1 K(+) channel.Semantic proximity Read ↗

Ring of negative charge in BK channels facilitates block by intracellular Mg2+ and polyamines through electrostatics.Semantic proximity Read ↗

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Three pairs of weak interactions precisely regulate the G-loop gate of Kir2.1 channel.Semantic proximity Read ↗

Mg(2+) binding to open and closed states can activate BK channels provided that the voltage sensors are elevated.Semantic proximity Read ↗

An inner-pore mutation (F315D) promotes intracellular Mg2+ block and inward rectification of BK channels.Semantic proximity Read ↗

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