ArticleThe Journal of biological chemistry2015
Yeast Fex1p Is a Constitutively Expressed Fluoride Channel with Functional Asymmetry of Its Two Homologous Domains.
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 31 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
31 citing papers in PubMed.
- Monovalent cations differentially regulate the activity of eukaryotic fluoride channels and impact fluoride resistance.PLoS biology · 2026Article
- Beyond Single Enzymes: System-Level Fungal Transformation of Halogenated Nitrophenols.Journal of fungi (Basel, Switzerland) · 2026Article
- CFTR and ClC-3 Transport Fluoride Differently and Cause Dental Fluorosis in Different Ways.Biomolecules · 2026Article
- Molecular Genetics and Probiotic Mechanisms of Saccharomyces cerevisiae var. boulardii.Probiotics and antimicrobial proteins · 2026Review
- Asymmetry-induced distinct mechanisms and the transporting role of sodium in bacterial fluoride channel Fluc.bioRxiv : the preprint server for biology · 2026Article
- The molecular mechanism of fluoride export by the eukaryotic fluoride channel FEX.Nature communications · 2025Article
- The link between ancient microbial fluoride resistance mechanisms and bioengineering organofluorine degradation or synthesis.Nature communications · 2024Review
- Article
- Fluoride export is required for competitive fitness of pathogenic microorganisms in dental biofilm models.bioRxiv : the preprint server for biology · 2024Article
- Lanthanum-fluoride electrode-based methods to monitor fluoride transport in cells and reconstituted lipid vesicles.Methods in enzymology · 2024Article
- The role of conformational change and key glutamic acid residues in the ClC-ec1 antiporter.Biophysical journal · 2023Article
- Article
- Ion permeation, selectivity, and electronic polarization in fluoride channels.Biophysical journal · 2022Article
- Article
- Membrane Exporters of Fluoride Ion.Annual review of biochemistry · 2021Review
- Saccharomyces cerevisiae Gene Expression during Fermentation of Pinot Noir Wines at an Industrially Relevant Scale.Applied and environmental microbiology · 2021Article
- The fluoride transporter FLUORIDE EXPORTER (FEX) is the major mechanism of tolerance to fluoride toxicity in plants.Plant physiology · 2021Article
- Genome-wide analysis of fluoride exporter genes in plants.3 Biotech · 2021Article
- The application of Poisson distribution statistics in ion channel reconstitution to determine oligomeric architecture.Methods in enzymology · 2021Article
- Former orphan riboswitches reveal unexplored areas of bacterial metabolism, signaling, and gene control processes.RNA (New York, N.Y.) · 2020Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors.
Funding
Abstract
Fluoride is a ubiquitous environmental toxin with which all biological species must cope. A recently discovered family of fluoride export (FEX) proteins protects organisms from fluoride toxicity by removing it from the cell. We show here that FEX proteins in Saccharomyces cerevisiae function as ion channels that are selective for fluoride over chloride and that these proteins are constitutively expressed at the yeast plasma membrane. Continuous expression is in contrast to many other toxin exporters in yeast, and this, along with the fact that two nearly duplicate proteins are encoded in the yeast genome, suggests that the threat posed by fluoride ions is frequent and detrimental. Structurally, eukaryotic FEX proteins consist of two homologous four-transmembrane helix domains folded into an antiparallel dimer, where the orientation of the two domains is fixed by a single transmembrane linker helix. Using phylogenetic sequence conservation as a guide, we have identified several functionally important residues. There is substantial functional asymmetry in the effect of mutation at corresponding sites in the two domains. Specifically, mutations to residues in the C-terminal domain proved significantly more detrimental to function than did similar mutations in the N-terminal domain. Our data suggest particular residues that may be important to anion specificity, most notably the necessity of a positive charge near the end of TMH1 in the C-terminal domain. It is possible that a cationic charge at this location may create an electrostatic well for fluoride ions entering the channel from the cytoplasm.
Indexed as
Identifiers
What OpenQuestion holds
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.