ArticleBiochimica et biophysica acta2011
Cholesterol regulates prokaryotic Kir channel by direct binding to channel protein.
Article in Biochimica et biophysica acta, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 53 citations in OpenAlex.
- Exploring lipid diversity and minimalism to define membrane requirements for synthetic cells.FEBS letters · 2025Review
- Cholesterol metabolism and intrabacterial potassium homeostasis are intrinsically related in Mycobacterium tuberculosis.PLoS pathogens · 2025Article
- The C. elegans LON-1 protein requires its CAP domain for function in regulating body size and BMP signaling.Genetics · 2025Article
- Endocannabinoid regulation of inward rectifier potassium (Kir) channels.Frontiers in pharmacology · 2024Article
- Cholesterol regulation of mechanosensitive ion channels.Frontiers in cell and developmental biology · 2024Review
- Membrane Cholesterol Interactions with Proteins in Hypercholesterolemia-Induced Endothelial Dysfunction.Current atherosclerosis reports · 2023Review
- Cholesterol-induced suppression of Kir2 channels is mediated by decoupling at the inter-subunit interfaces.iScience · 2022Article
- A Cholesterol Dimer Stabilizes the Inactivated State of an Inward-Rectifier Potassium Channel.Angewandte Chemie (International ed. in English) · 2022Article
- Cell-Free Expression of Proton-Coupled Folate Transporter in the Presence of Nanodiscs.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Cholesterol-Induced Suppression of Endothelial Kir Channels Is a Driver of Impairment of Arteriolar Flow-Induced Vasodilation in Humans.Hypertension (Dallas, Tex. : 1979) · 2022Article
- Distinct lipid bilayer compositions have general and protein-specific effects on K+ channel function.The Journal of general physiology · 2021Article
- Impact of nanodisc lipid composition on cell-free expression of proton-coupled folate transporter.PloS one · 2021Article
- Impairment of Flow-Sensitive Inwardly Rectifying KArteriosclerosis, thrombosis, and vascular biology · 2020Article
- Defining how multiple lipid species interact with inward rectifier potassium (Kir2) channels.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Comparative docking analysis of cholesterol analogs to ion channels to discriminate between stereospecific binding vs. stereospecific response.Channels (Austin, Tex.) · 2019Article
- An Inward-Rectifier Potassium Channel Coordinates the Properties of Biologically Derived Membranes.Biophysical journal · 2019Article
- Modulation of Transient Receptor Potential C Channel Activity by Cholesterol.Frontiers in pharmacology · 2019Review
- Constitutive boost of a KProceedings of the National Academy of Sciences of the United States of America · 2018Article
- Molecular Dynamics Simulations of Kir2.2 Interactions with an Ensemble of Cholesterol Molecules.Biophysical journal · 2018Article
- Challenges and approaches to understand cholesterol-binding impact on membrane protein function: an NMR view.Cellular and molecular life sciences : CMLS · 2018Review
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Cholesterol is a major regulator of a variety of ion channels but the mechanisms underlying cholesterol sensitivity of ion channels are still poorly understood. The key question is whether cholesterol regulates ion channels by direct binding to the channel protein or by altering the physical environment of lipid bilayer. In this study, we provide the first direct evidence that cholesterol binds to prokaryotic Kir channels, KirBac1.1, and that cholesterol binding is essential for its regulatory effect. Specifically, we show that cholesterol is eluted together with the KirBac1.1 protein when separated on an affinity column and that the amount of bound cholesterol is proportional to the amount of the protein. We also show that cholesterol binding to KirBac1.1 is saturable with a K(D) of 390μM. Moreover, there is clear competition between radioactive and non-radioactive cholesterol for the binding site. There is no competition, however, between cholesterol and 5-Androsten 3β-17 β-diol, a sterol that we showed previously to have no effect on KirBac1.1 function. Finally, we show that cholesterol-KirBac1.1 binding is significantly inhibited by trifluoperazine, known to inhibit cholesterol binding to other proteins, and that inhibition of cholesterol-KirBac1.1 binding results in full recovery of the channel activity. Collectively, results from this study indicate that cholesterol-induced suppression of KirBac1.1 activity is mediated by direct interaction between cholesterol and the channel protein.
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Registered trials
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