ArticleProceedings of the National Academy of Sciences of the United States of America2015
Two-sided block of a dual-topology F- channel.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
What it found
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Who cites it
18 citing papers in PubMed, 24 citations in OpenAlex.
- The molecular mechanism of fluoride export by the eukaryotic fluoride channel FEX.Nature communications · 2025Article
- Fluoride permeation mechanism of the Fluc channel in liposomes revealed by solid-state NMR.Science advances · 2023Article
- Controlling ion channel function with renewable recombinant antibodies.The Journal of physiology · 2022Review
- Ion permeation, selectivity, and electronic polarization in fluoride channels.Biophysical journal · 2022Article
- Article
- Membrane Exporters of Fluoride Ion.Annual review of biochemistry · 2021Review
- High-Throughput Screening of Protein-Detergent Complexes Using Fluorescence Polarization Spectroscopy.Current protocols in protein science · 2019Article
- Cork-in-Bottle Occlusion of Fluoride Ion Channels by Crystallization Chaperones.Structure (London, England : 1993) · 2018Article
- Reconstitution and functional characterization of ion channels from nanodiscs in lipid bilayers.The Journal of general physiology · 2018Article
- Molecular Interactions between a Fluoride Ion Channel and Synthetic Protein Blockers.Biochemistry · 2018Article
- Assigning crystallographic electron densities with free energy calculations-The case of the fluoride channel Fluc.PloS one · 2018Article
- Quantification of Membrane Protein-Detergent Complex Interactions.The journal of physical chemistry. B · 2017Article
- Article
- Interrogating Detergent Desolvation of Nanopore-Forming Proteins by Fluorescence Polarization Spectroscopy.Analytical chemistry · 2017Article
- A topologically diverse family of fluoride channels.Current opinion in structural biology · 2017Review
- Protein ligands for studying ion channel proteins.The Journal of general physiology · 2017Article
- Mechanism of single- and double-sided inhibition of dual topology fluoride channels by synthetic monobodies.The Journal of general physiology · 2017Article
- Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
The Fluc family is a set of small membrane proteins forming F(-)-specific electrodiffusive ion channels that rescue microorganisms from F(-) toxicity during exposure to weakly acidic environments. The functional channel is built as a dual-topology homodimer with twofold symmetry parallel to the membrane plane. Fluc channels are blocked by nanomolar-affinity fibronectin-domain monobodies originally selected from phage-display libraries. The unusual symmetrical antiparallel dimeric architecture of Flucs demands that the two chemically equivalent monobody-binding epitopes reside on opposite ends of the channel, a double-sided blocking situation that has never before presented itself in ion channel biophysics. However, it is not known if both sites can be simultaneously occupied, and if so, whether monobodies bind independently or cooperatively to their transmembrane epitopes. Here, we use direct monobody-binding assays and single-channel recordings of a Fluc channel homolog to reveal a novel trimolecular blocking behavior that reveals a doubly occupied blocked state. Kinetic analysis of single-channel recordings made with monobody on both sides of the membrane shows substantial negative cooperativity between the two blocking sites.
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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.