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Article

Reciprocal regulation of the Ca2+ and H+ sensitivity in the SLO1 BK channel conferred by the RCK1 domain.

Nature structural & molecular biology - 1 Apr 2008

Hou Shangwei, Xu Rong, Heinemann Stefan H, Hoshi Toshinori

Abstract excerpt

Increasing evidence suggests that intracellular H+ directly stimulates large-conductance Ca2+- and voltage-activated K+ (SLO1 BK) channels, thus providing a crucial link between membrane excitability and cell metabolism. Here we report that two histidine residues, His365 and His394, located in th...

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Identifiers

PMID: 18345016
DOI: 10.1038/nsmb.1398
PMCID: PMC2905141

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-18345016-2026-09-02.2. 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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Research trail→

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Reciprocal regulation of the Ca2+ and H+ sensitivity in the SLO1 BK channel conferred by the RCK1 domain.PMID 18345016Read ↗

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The RCK2 domain uses a coordination site present in Kir channels to confer sodium sensitivity to Slo2.2 channels.Semantic proximity Read ↗

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Haem can bind to and inhibit mammalian calcium-dependent Slo1 BK channels.Semantic proximity Read ↗

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Three methionine residues located within the regulator of conductance for K+ (RCK) domains confer oxidative sensitivity to large-conductance Ca2+-activated K+ channels.Semantic proximity Read ↗

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