ArticleCommunications biology2022
The roles of two extracellular loops in proton sensing and permeation in human Otop1 proton channel.
Article in Communications biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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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.
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Who cites it
11 citing papers in PubMed, 18 citations in OpenAlex.
- Human OTOP3 requires strong acidification for activation and exhibits mixed proton-anion permeation.The Journal of biological chemistry · 2026Article
- Structure-guided discovery of Otopetrin 1 inhibitors reveals druggable binding sites at the intrasubunit interface.Nature communications · 2025Article
- OTOP3 functions as an oncogenic regulator of ferroptosis-mediated colorectal cancer progression.Genes & genomics · 2025Article
- Adaptive Responses of Large Yellow CroakerAntioxidants (Basel, Switzerland) · 2025Article
- Molecular mechanism of pH sensing and activation in GPR4 reveals proton-mediated GPCR signaling.Cell discovery · 2025Article
- 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
- Gating elements for carvacrol activation of the OTOP1 proton channel.Communications biology · 2024Article
- Transcendent Aspects of Proton Channels.Annual review of physiology · 2024Review
- 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 1 institution in 1 country.
Funding
Abstract
Otopetrin (Otop) proteins were recently found to function as proton channels, with Otop1 revealed to be the sour taste receptor in mammals. Otop proteins contain twelve transmembrane segments (S1-S12) which are divided into structurally similar N and C domains. The mechanisms by which Otop channels sense extracellular protons to initiate gating and conduct protons once the channels are activated remains largely elusive. Here we show that two extracellular loops are playing key roles in human Otop1 channel function. We find that residue H229 in the S5-S6 loop is critical for proton sensing of Otop1. Further, our data reveal that the S11-12 loop is structurally and functionally essential for the Otop1 channel and that residue D570 in this loop regulates proton permeation into the pore formed by the C domain. This study sheds light on the molecular mechanism behind the structure and function of this newly identified ion channel family.
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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.