ArticleNature structural & molecular biology2019
Structures of the otopetrin proton channels Otop1 and Otop3.
Article in Nature structural & molecular biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
What it found
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Who cites it
46 citing papers in PubMed, 73 citations in OpenAlex.
- Human OTOP3 requires strong acidification for activation and exhibits mixed proton-anion permeation.The Journal of biological chemistry · 2026Article
- Otopetrin 1 protects against adipose tissue wasting during cancer cachexia progression.iScience · 2026Article
- Genome-wide association study of molecular markers related to keel length in a specialized strain of yellow feathered broilers.Poultry science · 2026Article
- Molecular and Computational Basis of Taste Perception: A Review toward the "Digital Language of Taste".ACS omega · 2026Review
- Structure-guided discovery of Otopetrin 1 inhibitors reveals druggable binding sites at the intrasubunit interface.Nature communications · 2025Article
- Artificial Nervous Systems.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Review
- Preferential allosteric modulation of Otop1 channels by small molecule compounds.Communications biology · 2025Article
- Epitope Tagging with Genome Editing in Mice Reveals That the Proton Channel OTOP1 Is Apically Localized and Not Restricted to Type III "Sour" Taste Receptor Cells.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2025Article
- Receptors and signaling for sour and salty: the ionic taste qualities.Chemical senses · 2025Review
- Development of the semicircular canals and otolithic organs of the vertebrate inner ear.Current topics in developmental biology · 2025Review
- Ectopic taste receptors in animal physiology: evolutionary conservation and functional diversification.Frontiers in cell and developmental biology · 2025Review
- Genetic analysis of non-syndromic peg lateralis using whole-exome sequencing.Frontiers in genetics · 2025Article
- Gating elements for carvacrol activation of the OTOP1 proton channel.Communications biology · 2024Article
- Duodenal transcriptomics demonstrates signatures of tissue inflammation and immune cell infiltration in children with environmental enteric dysfunction across global centers.The American journal of clinical nutrition · 2024Article
- Structural, Functional and Molecular Dynamics Examination of a de novo cloned Otopetrin-like Proton Channel in crayfish.Cell biochemistry and biophysics · 2024Article
- Structural mechanism of proton conduction in otopetrin proton channel.Nature communications · 2024Article
- Transcendent Aspects of Proton Channels.Annual review of physiology · 2024Review
- Determination of the Immunomodulatory Role of OTOP2 in Colon Adenocarcinoma.Journal of Cancer · 2024Article
- LipIDens: simulation assisted interpretation of lipid densities in cryo-EM structures of membrane proteins.Nature communications · 2023Article
- The proton channel OTOP1 is a sensor for the taste of ammonium chloride.Nature communications · 2023Article
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
Abstract
Otopetrins (Otop1-Otop3) comprise one of two known eukaryotic proton-selective channel families. Otop1 is required for otoconia formation and a candidate mammalian sour taste receptor. Here we report cryo-EM structures of zebrafish Otop1 and chicken Otop3 in lipid nanodiscs. The structures reveal a dimeric architecture, with each subunit forming 12 transmembrane helices divided into structurally similar amino (N) and carboxy (C) domains. Cholesterol-like molecules occupy various sites in Otop1 and Otop3 and occlude a central tunnel. In molecular dynamics simulations, hydrophilic vestibules formed by the N and C domains and in the intrasubunit interface between N and C domains form conduits for water entry into the membrane core, suggesting three potential proton conduction pathways. By mutagenesis, we tested the roles of charged residues in each putative permeation pathway. Our results provide a structural basis for understanding selective proton permeation and gating of this conserved family of proton channels.
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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.