ArticleFood chemistry. Molecular sciences2025
Inosine-5'-monophosphate interacts with the TAS1R3 subunit to enhance sweet taste detection.
Article in Food chemistry. Molecular sciences, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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6 citing papers in PubMed.
- Investigation of the effects and underlying mechanisms of adenylate kinase 1 on inosine monophosphate deposition in Beijing-You chickens.Poultry science · 2026Article
- A comparison of physicochemical and flavor properties of species on surimi gels fromFood chemistry: X · 2026Article
- Sweet and umami TAS1R receptors: from molecular recognition to physiological function.Chemical senses · 2026Review
- Dietary responses of taste receptor genes to plant-based diets in farmed fish: A literature review.Open veterinary journal · 2026Review
- Glutathione as a taste modulator: molecular mechanisms of interaction with umami and sweet taste receptors.Food chemistry. Molecular sciences · 2025Article
- Effects of dietary supplementation with hydroponic wheat seedlings on rumen fermentation, meat quality, amino acid and fatty acid contents, and rumen bacterial diversity in sheep.Frontiers in microbiology · 2025Article
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Abstract
Umami and sweet taste detection is mediated by the activation of the TAS1R1/TAS1R3 and TAS1R2/TAS1R3 receptors, respectively. TAS1R2-Venus flytrap domain (VFT) constitutes the primary ligand-binding site for most of the sweeteners whereas TAS1R1-VFT contains the orthosteric binding site for umami compounds. Inosine-5'-monophosphate (IMP), previously known to potentiate umami taste, binds to a site of TAS1R1-VFT adjacent to the L-glutamate site leading to umami synergy. However, the involvement of the TAS1R3 subunit in umami receptor-ligand interactions or in synergy with IMP has never been demonstrated. To elucidate the VFT contribution to umami and sweet detection, we expressed human TAS1R1- and TAS1R3-VFTs in bacteria. Ligand binding studies quantified by intrinsic tryptophan fluorescence revealed that both TAS1R1- and TAS1R3-VFTs are able to interact with umami compounds. Cellular assays revealed that IMP is able, like cyclamate, to modulate the response of TAS1R2/TAS1R3 and TAS1R3 alone stimulated by calcium ions. IMP also acted as an enhancer of TAS1R2/TAS1R3 when stimulated with sucralose, neotame and cyclamate. Taking together, our data demonstrated that IMP modulates sweet compound detection at the receptor level acting via the TAS1R3 subunit. This research suggests more complex receptor interactions between umami and sweet taste qualities and paves the way for development of new sweetness enhancers.
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