ArticleNature communications2019
Structural basis for functional interactions in dimers of SLC26 transporters.
Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 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
40 citing papers in PubMed.
- The SLC-ome of membrane transport: from molecular discovery to physiology and clinical applications.Physiological reviews · 2026Review
- The ZBTB16/CUL3/ROC1 ubiquitin ligase drives the degradation of pathogenic pendrin (SLC26A4) protein variants.Journal of biomedical science · 2026Article
- Structural and dynamic insights into SPDT for phosphorus allocation in rice.Science China. Life sciences · 2026Article
- Lactylation of SLC26A3 in the acidic tumor microenvironment promotes malignant progression of colorectal carcinoma.Cell death & disease · 2026Article
- Structural Mechanism of Prestin-Membrane Mechanotransduction.bioRxiv : the preprint server for biology · 2025Article
- Protein Modeling with DEER Spectroscopy.Annual review of biophysics · 2025Review
- Molecular insights into the elevator-type mechanism of the cyanobacterial bicarbonate transporter BicA.Biophysical journal · 2025Article
- Analysis of the sulfate permease family inFrontiers in plant science · 2025Article
- Insights into Transient Dimerisation of Carnitine/Acylcarnitine Carrier (SLC25A20) from Sarkosyl/PAGE, Cross-Linking Reagents, and Comparative Modelling Analysis.Biomolecules · 2024Article
- Interdomain-linkers control conformational transitions in the SLC23 elevator transporter UraA.Nature communications · 2024Article
- Structural and biophysical analysis of aeLife · 2024Article
- SLC26 Anion Transporters.Handbook of experimental pharmacology · 2024Review
- Elevator-like movements of prestin mediate outer hair cell electromotility.Nature communications · 2023Article
- Membrane-anchored substrate binding proteins are deployed in secondary TAXI transporters.Biological chemistry · 2023Article
- Borate Transporters and SLC4 Bicarbonate Transporters Share Key Functional Properties.Membranes · 2023Article
- SLC26 family: a new insight for kidney stone disease.Frontiers in physiology · 2023Review
- Lipid-mediated prestin organization in outer hair cell membranes and its implications in sound amplification.Nature communications · 2022Article
- Dominant negative mutation in oxalate transporterJournal of medical genetics · 2022Article
- Cryo-EM structures of thermostabilized prestin provide mechanistic insights underlying outer hair cell electromotility.Nature communications · 2022Article
- Homodimerized cytoplasmic domain of PD-L1 regulates its complex glycosylation in living cells.Communications biology · 2022Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The SLC26 family of transporters maintains anion equilibria in all kingdoms of life. The family shares a 7 + 7 transmembrane segments inverted repeat architecture with the SLC4 and SLC23 families, but holds a regulatory STAS domain in addition. While the only experimental SLC26 structure is monomeric, SLC26 proteins form structural and functional dimers in the lipid membrane. Here we resolve the structure of an SLC26 dimer embedded in a lipid membrane and characterize its functional relevance by combining PELDOR/DEER distance measurements and biochemical studies with MD simulations and spin-label ensemble refinement. Our structural model reveals a unique interface different from the SLC4 and SLC23 families. The functionally relevant STAS domain is no prerequisite for dimerization. Characterization of heterodimers indicates that protomers in the dimer functionally interact. The combined structural and functional data define the framework for a mechanistic understanding of functional cooperativity in SLC26 dimers.
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.