ArticlePflugers Archiv : European journal of physiology2011
Cysteine residue 911 in C-terminal tail of human BK(Ca)α channel subunit is crucial for its activation by carbon monoxide.
Article in Pflugers Archiv : European journal of physiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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23 citing papers in PubMed, 41 citations in OpenAlex.
- Potassium channels in vascular smooth muscle cells.Physiological reviews · 2026Review
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- Cannabidiol Protects Dopaminergic Neurons in Mesencephalic Cultures against the Complex I Inhibitor Rotenone Via Modulation of Heme Oxygenase Activity and Bilirubin.Antioxidants (Basel, Switzerland) · 2020Article
- Targeting the Heme Oxygenase 1/Carbon Monoxide Pathway to Resolve Lung Hyper-Inflammation and Restore a Regulated Immune Response in Cystic Fibrosis.Frontiers in pharmacology · 2020Review
- Role of Heme Oxygenase as a Modulator of Heme-Mediated Pathways.Antioxidants (Basel, Switzerland) · 2019Review
- Carbon monoxide in lung cell physiology and disease.American journal of physiology. Cell physiology · 2018Review
- CO-independent modification of KEuropean journal of pharmacology · 2017Article
- Mechanistic insight into the heme-independent interplay between iron and carbon monoxide in CFTR and Slo1 BKMetallomics : integrated biometal science · 2017Review
- Carbon monoxide releasing molecule-2 inhibition of snake venom thrombin-like activity: novel biochemical "brake"?Journal of thrombosis and thrombolysis · 2017Article
- Carbon Monoxide Modulates Connexin Function through a Lipid Peroxidation-Dependent Process: A Hypothesis.Frontiers in physiology · 2016Article
- Diverse mechanisms underlying the regulation of ion channels by carbon monoxide.British journal of pharmacology · 2015Review
- Extracellular hemoglobin: the case of a friend turned foe.Frontiers in physiology · 2015Review
- Carbon monoxide (CO) is a novel inhibitor of connexin hemichannels.The Journal of biological chemistry · 2014Article
- Big Potassium (BK) ion channels in biology, disease and possible targets for cancer immunotherapy.International immunopharmacology · 2014Review
- Carbon monoxide--physiology, detection and controlled release.Chemical communications (Cambridge, England) · 2014Review
- Review article: carbon monoxide in gastrointestinal physiology and its potential in therapeutics.Alimentary pharmacology & therapeutics · 2013Review
- Heme sensor proteins.The Journal of biological chemistry · 2013Review
- Neuroprotective, neurotherapeutic, and neurometabolic effects of carbon monoxide.Medical gas research · 2012Article
- Function and regulation of large conductance Ca(2+)-activated K+ channel in vascular smooth muscle cells.Drug discovery today · 2012Review
- Therapeutic potential of heme oxygenase-1/carbon monoxide in lung disease.International journal of hypertension · 2012Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
The large conductance, voltage- and calcium-activated potassium channel, BK(Ca), is a known target for the gasotransmitter, carbon monoxide (CO). Activation of BK(Ca) by CO modulates cellular excitability and contributes to the physiology of a diverse array of processes, including vascular tone and oxygen-sensing. Currently, there is no consensus regarding the molecular mechanisms underpinning reception of CO by the BK(Ca). Here, employing voltage-clamped, inside-out patches from HEK293 cells expressing single, double and triple cysteine mutations in the BK(Ca) α-subunit, we test the hypothesis that CO regulation is conferred upon the channel by interactions with cysteine residues within the RCK2 domain. In physiological [Ca(2+)](i), all mutants carrying a cysteine substitution at position 911 (C911G) demonstrated significantly reduced CO sensitivity; the C911G mutant did not express altered Ca(2+)-sensitivity. In contrast, histidine residues in RCK1 domain, previously shown to ablate CO activation in low [Ca(2+)](i), actually increased CO sensitivity when [Ca(2+)](i) was in the physiological range. Importantly, cyanide, employed here as a substituent for CO at potential metal centres, occluded activation by CO; this effect was freely reversible. Taken together, these data suggest that a specific cysteine residue in the C-terminal domain, which is close to the Ca(2+) bowl but which is not involved in Ca(2+) activation, confers significant CO sensitivity to BK(Ca) channels. The rapid reversibility of CO and cyanide binding, coupled to information garnered from other CO-binding proteins, suggests that C911 may be involved in formation of a transition metal cluster which can bind and, thereafter, activate BK(Ca).
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.