ArticleThe Journal of biological chemistry2015
Membrane Potential Controls the Efficacy of Catecholamine-induced β1-Adrenoceptor Activity.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 29 citations in OpenAlex.
- Interactions between extracellular vesicles and hormones: review.Animal bioscience · 2026Article
- The gut microbiome promotes detoxification responses to an environmental toxicant.bioRxiv : the preprint server for biology · 2025Article
- Charge Movements and Conformational Changes: Biophysical Properties and Physiology of Voltage-Dependent GPCRs.Biomolecules · 2024Review
- Voltage Sensors Embedded in G Protein-Coupled Receptors.International journal of molecular sciences · 2024Review
- Article
- Functional consequences of a rare human serotonergic 5-HTFrontiers in pharmacology · 2023Article
- G Protein-Coupled Receptors Regulated by Membrane Potential.International journal of molecular sciences · 2022Review
- The activity of the serotonergic 5-HTThe Journal of biological chemistry · 2022Article
- Mechanical and chemical activation of GPR68 probed with a genetically encoded fluorescent reporter.Journal of cell science · 2021Article
- Voltage modulates the effect of μ-receptor activation in a ligand-dependent manner.British journal of pharmacology · 2020Article
- Sodium ions allosterically modulate the M2 muscarinic receptor.Scientific reports · 2020Article
- Voltage-Dependent Dopamine Potency at DFrontiers in pharmacology · 2020Article
- Helix 8 is the essential structural motif of mechanosensitive GPCRs.Nature communications · 2019Article
- Harnessing Ion-Binding Sites for GPCR Pharmacology.Pharmacological reviews · 2019Review
- Article
- Thermodynamic secrets of multidrug resistance: A new take on transport mechanisms of secondary active antiporters.Protein science : a publication of the Protein Society · 2018Review
- Dynamic monitoring of GPflugers Archiv : European journal of physiology · 2017Article
- Thermodynamics of GPCR activation.Biophysics reportsArticle
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
G protein-coupled receptors (GPCRs) are membrane-located proteins and, therefore, are exposed to changes in membrane potential (V(M)) in excitable tissues. These changes have been shown to alter receptor activation of certain Gi-and Gq-coupled GPCRs. By means of a combination of whole-cell patch-clamp and Förster resonance energy transfer (FRET) in single cells, we demonstrate that the activation of the Gs-coupled β1-adrenoreceptor (β1-AR) by the catecholamines isoprenaline (Iso) and adrenaline (Adr) is regulated by V(M). This voltage-dependence is also transmitted to G protein and arrestin 3 signaling. Voltage-dependence of β2-AR activation, however, was weak compared with β1-AR voltage-dependence. Drug efficacy is a major target of β1-AR voltage-dependence as depolarization attenuated receptor activation, even under saturating concentrations of agonists, with significantly faster kinetics than the deactivation upon agonist withdrawal. Also the efficacy of the endogenous full agonist adrenaline was reduced by depolarization. This is a unique finding since reports of natural full agonists at other voltage-dependent GPCRs only show alterations in affinity during depolarization. Based on a Boltzmann function fit to the relationship of V(M) and receptor-arrestin 3 interaction we determined the voltage-dependence with highest sensitivity in the physiological range of membrane potential. Our data suggest that under physiological conditions voltage regulates the activity of agonist-occupied β1-adrenoceptors on a very fast time scale.
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Registered trials
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.