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Eukaryotic resistance to fluoride toxicity mediated by a widespread family of fluoride export proteins
Abstract
Significance: Although fluoride is plentiful in the environment and is commonly used at high concentrations in oral hygiene products, little has been known about how biological systems overcome the toxic effects of this anion. We demonstrate that a protein called FEX in many fungi is essential for cell survival in the presence of high fluoride concentrations. The protein is required for the rapid expulsion of cytoplasmic fluoride, indicating that many eukaryotic species that carry FEX genes likely avoid fluoride toxicity by purging cellular fluoride.
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CrcB export proteins function as passive fluoride-specific ion channels that require Na+ ions for transport activity.
“In contrast, CrcB export proteins function as passive fluoride-specific ion channels that require Na+ ions for transport activity (4, 5, 23–26).”
From Adaptive evolution of Pseudomonas putida in the presence of fluoride exposes novel functions of a benzoate transporter (2026) · cites this paper as [24]
Candida albicans extrudes intracellular fluoride using a FEX fluoride channel.
“Eukaryotes, including C. albicans, express a third type of fluoride exporter called FEX (Fluoride Exporter) (18).”
From Fluoride export is required for the competitive fitness of pathogenic microorganisms in dental biofilm models (2024) · cites this paper as [18]
Genetic knockout of fluoride exporters causes fluoride hypersensitivity in multiple species, including oral microbiota, reducing the inhibitory concentration of fluoride to the tens-to-hundreds of micromolar range.
“Genetic knockout of fluoride exporters causes fluoride hypersensitivity in multiple species, including oral microbiota, reducing the inhibitory concentration of fluoride to the tens-to-hundreds of micromolar range (17–19).”
From Fluoride export is required for the competitive fitness of pathogenic microorganisms in dental biofilm models (2024) · cites this paper as [18]
Eukaryotes, including C. albicans, express a third type of fluoride exporter called FEX.
“Eukaryotes, including C. albicans, express a third type of fluoride exporter called FEX (Fluoride Exporter) (18).”
From Fluoride export is required for the competitive fitness of pathogenic microorganisms in dental biofilm models (2024) · cites this paper as [18]
Fluoride acts as a bacteriostatic agent for many microbes.
“Whereas fluoride acts as a bacteriostatic agent for many microbes (18, 20, 46)”
From Fluoride export is required for the competitive fitness of pathogenic microorganisms in dental biofilm models (2024) · cites this paper as [18]
Yeast, fungi, plants, and some ocean-dwelling animals possess fluoride exporters of the FEX family.
“Yeast, fungi, plants, and some ocean-dwelling animals like corals and sponges also possess fluoride exporters that belong to a third molecular family known as FEX85,86.”
From The link between ancient microbial fluoride resistance mechanisms and bioengineering organofluorine degradation or synthesis (2024) · cites this paper as [85]
Fluc proteins are F--specific ion channels of the Fluc family.
“microorganisms export this anion through F--specific ion channels of the Fluc family1–4.”
From Crystal structures of a double-barrelled fluoride ion channel (2015) · cites this paper as [2]
Unicellular organisms counteract F- toxicity through F--exporting membrane transport proteins that keep cytoplasmic F- below inhibitory levels.
“Unicellular organisms directly exposed to environmental F- counteract the anion’s toxicity through the action of F--exporting membrane transport proteins that keep cytoplasmic F- below inhibitory levels1–4,8.”
From Crystal structures of a double-barrelled fluoride ion channel (2015) · cites this paper as [2]
Expression of F− export proteins in the plasma membrane undermines weak acid accumulation of fluoride.
“By providing a route for accumulating F− to exit the cell, expression of these F− export proteins in the plasma membrane simply undermines weak acid accumulation of fluoride (1, 14, 25, 26).”
From Membrane exporters of fluoride ion (2021) · cites this paper as [26]
Eukaryotic FEX proteins, like CLCF proteins, have an inverted repeat architecture, in which two structurally homologous domains in a single polypeptide are arranged in opposite orientations.
“The eukaryotic FEX proteins, like the CLCF proteins, have an inverted repeat architecture, in which two structurally homologous domains in a single polypeptide are arranged in opposite orientations(3, 26).”
From Membrane exporters of fluoride ion (2021) · cites this paper as [26]
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Crystal structures of a double-barrelled fluoride ion channel
Stockbridge, R. B., Kolmakova-Partensky, L., Shane, T., Koide, A., Koide, S., Miller, C., & Newstead, S. (2015) · Nature · doi:10.1038/nature14981 · Cited by 119
Bacterial fluoride resistance, Fluc channels, and the weak acid accumulation effect
Ji, C., Stockbridge, R. B., & Miller, C. (2014) · Journal of General Physiology · doi:10.1085/jgp.201411243 · Cited by 97
Stockbridge, R. B., & Wackett, L. P. (2024) · Nature Communications · doi:10.1038/s41467-024-49018-1 · Cited by 80
Membrane exporters of fluoride ion
McIlwain, B. C., Ruprecht, M. T., & Stockbridge, R. B. (2021) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-071520-112507 · Cited by 69
Small Molecule Fluoride Toxicity Agonists
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Destruction Of C7, C9 Perfluorocarboxylic Acids By The Strain Ensifer Adhaerens M1
Hkudaigulov, G., Sharipov, D., Starikov, S., & Chetverikov, S. (2024) · Malaysian Journal of Fundamental and Applied Sciences · doi:10.11113/mjfas.v20n6.3655
Metadata
- Authors
- Li, S., Smith, K. D., Davis, J. H., Gordon, P. B., Breaker, R. R., & Strobel, S. A.
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2013-10-30
- Volume
- 110
- Issue
- 47
- Pages
- 19018-19023
- ISSN
- 0027-8424
- 1091-6490
- Cited by
- 122
- References
- 1
- Language
- en
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