ArticleThe Journal of biological chemistry2004
Functional characterization of a prokaryotic Kir channel.
Article in The Journal of biological chemistry, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed, 56 citations in OpenAlex.
- Planar Lipid Bilayers and Liposomes: Essential Models for Advancing Protein Structure and Function Research.Advances in experimental medicine and biology · 2026Review
- Anionic lipids modulate the membrane localization and conformational dynamics of KirBac1.1 slide helix during lipid-dependent activation.The Biochemical journal · 2025Article
- Structural Dynamics of the Slide Helix of Inactive/Closed Conformation of KirBac1.1 in Micelles and Membranes: A Fluorescence Approach.The Journal of membrane biology · 2025Article
- pH-induced conformational changes in the selectivity filter of a potassium channel lead to alterations in its selectivity and permeation properties.Frontiers in pharmacology · 2024Article
- Article
- A Cholesterol Dimer Stabilizes the Inactivated State of an Inward-Rectifier Potassium Channel.Angewandte Chemie (International ed. in English) · 2022Article
- Pore-forming transmembrane domains control ion selectivity and selectivity filter conformation in the KirBac1.1 potassium channel.The Journal of general physiology · 2021Article
- Inwardly rectifying potassium channel 5.1: Structure, function, and possible roles in diseases.Genes & diseases · 2021Review
- FRET-based Microscopy Assay to Measure Activity of Membrane Amino Acid Transporters with Single-transporter Resolution.Bio-protocol · 2021Article
- Water Accessibility Refinement of the Extended Structure of KirBac1.1 in the Closed State.Frontiers in molecular biosciences · 2021Article
- The application of Poisson distribution statistics in ion channel reconstitution to determine oligomeric architecture.Methods in enzymology · 2021Article
- The Lipid Activation Mechanism of a Transmembrane Potassium Channel.Journal of the American Chemical Society · 2020Article
- Conformational changes upon gating of KirBac1.1 into an open-activated state revealed by solid-state NMR and functional assays.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- An Inward-Rectifier Potassium Channel Coordinates the Properties of Biologically Derived Membranes.Biophysical journal · 2019Article
- Potassium channel selectivity filter dynamics revealed by single-molecule FRET.Nature chemical biology · 2019Article
- Structural basis for the ethanol action on G-protein-activated inwardly rectifying potassium channel 1 revealed by NMR spectroscopy.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Conformational changes at cytoplasmic intersubunit interactions control Kir channel gating.The Journal of biological chemistry · 2017Article
- Solution-Based Single-Molecule FRET Studies of K(+) Channel Gating in a Lipid Bilayer.Biophysical journal · 2016Article
- Structural dynamics of potassium-channel gating revealed by single-molecule FRET.Nature structural & molecular biology · 2016Article
- Modular Design of the Selectivity Filter Pore Loop in a Novel Family of Prokaryotic 'Inward Rectifier' (NirBac) channels.Scientific reports · 2015Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
The Kir gene family encodes inward rectifying K+ (Kir) channels that are widespread and critical regulators of excitability in eukaryotic cells. A related gene family (KirBac) has recently been identified in prokaryotes. While a crystal structure of one member, Kir-Bac1.1, has been solved, there has been no functional characterization of any KirBac gene products. Here we present functional characterization of KirBac1.1 reconstituted in liposomes. Utilizing a 86Rb+ uptake assay, we demonstrate that KirBac1.1 generates a K+ -selective permeation path that is inhibited by extraliposomal Ba2+ and Ca2+ ions. In contrast to KcsA (an acid-activated bacterial potassium channel), KirBac1.1 is inhibited by extraliposomal acid (pKa approximately 6). This characterization of KirBac1.1 activity now paves the way for further correlation of structure and function in this model Kir channel.
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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.