ArticleNature communications2023
Asymmetric pendrin homodimer reveals its molecular mechanism as anion exchanger.
Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 27 citations in OpenAlex.
- The ZBTB16/CUL3/ROC1 ubiquitin ligase drives the degradation of pathogenic pendrin (SLC26A4) protein variants.Journal of biomedical science · 2026Article
- SLC26A11 is an atypical solute carrier with dual transport-channel function mediating lysosomal sulfate transport.Nature communications · 2026Article
- Identification of a novel isoform of Slc26a4 by single-cell RNA-sequencing of pendrin-expressing cells in the cochlea.Human genetics · 2026Article
- Mutational spectrum of SLC26A4 and SLC26A5 associated with hereditary hearing loss in Moroccan families.Human genomics · 2026Article
- Structural and dynamic insights into SPDT for phosphorus allocation in rice.Science China. Life sciences · 2026Article
- Molecular diagnosis of non-syndromic hearing loss in seven Iranian families using whole-exome sequencing.BMC medical genomics · 2026Article
- Structural Mechanism of Prestin-Membrane Mechanotransduction.bioRxiv : the preprint server for biology · 2025Article
- Asymmetric Dynamics Between the Protomers of the σ2 Receptor Homodimer.Journal of chemical information and modeling · 2025Article
- Molecular mechanism underlying phosphate distribution by SULTR family transporter SPDT inScience advances · 2025Article
- The SLC-ome of membrane transport: From molecular discovery to physiology and clinical applications.Physiological reviews · 2025Review
- Structural basis for substrate recognition mechanism of human SLC26A7.Nature communications · 2025Article
- Genetic heterogeneity in patients with enlarged vestibular aqueduct and Pendred syndrome.Molecular medicine (Cambridge, Mass.) · 2025Article
- Genetics of primary congenital hypothyroidism: three decades of discoveries and persisting etiological challenges.European thyroid journal · 2025Review
- Research hotspots and trends of theIntractable & rare diseases research · 2025Article
- High potency 3-carboxy-2-methylbenzofuran pendrin inhibitors as novel diuretics.European journal of medicinal chemistry · 2025Article
- CRISPR/Cas9-mediated exon skipping to restore premature translation termination in a DFNB4 mouse model.Gene therapy · 2024Article
- SLC26A4-AP-2 mu2 interaction regulates SLC26A4 plasma membrane abundance in the endolymphatic sac.Science advances · 2024Article
- Chloride/Multiple Anion Exchanger SLC26A Family: Systemic Roles of SLC26A4 in Various Organs.International journal of molecular sciences · 2024Review
- Vertigo During Pregnancy: A Narrative Review of the Etiology, Pathophysiology, and Treatment.Cureus · 2024Review
- Functional Studies of Deafness-Associated Pendrin and Prestin Variants.International journal of molecular sciences · 2024Article
Corrections and comments
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Authors and funding
18 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Pendrin (SLC26A4) is an anion exchanger expressed in the apical membranes of selected epithelia. Pendrin ablation causes Pendred syndrome, a genetic disorder associated with sensorineural hearing loss, hypothyroid goiter, and reduced blood pressure. However its molecular structure has remained unknown, limiting our understanding of the structural basis of transport. Here, we determine the cryo-electron microscopy structures of mouse pendrin with symmetric and asymmetric homodimer conformations. The asymmetric homodimer consists of one inward-facing protomer and the other outward-facing protomer, representing coincident uptake and secretion- a unique state of pendrin as an electroneutral exchanger. The multiple conformations presented here provide an inverted alternate-access mechanism for anion exchange. The structural and functional data presented here disclose the properties of an anion exchange cleft and help understand the importance of disease-associated variants, which will shed light on the pendrin exchange mechanism.
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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.