Evidence map›Paper›PMID 40715293›Full record

ArticleScientific reports2025

Distinct potency of compounds targeting the T1R3 subunit in modulating the response of human sweet and umami taste receptors.

Maiko Kawasaki, Yuta Kidera, Ryusei Goda, Chiaki Taketani, Misato Ide, Wataru Fujii, Tomoya Nakagita, Takumi Misaka

Abstract read
In one paragraph

Article in Scientific reports, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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.

2 · The registry

The trial behind it

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Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

1 citing paper in PubMed.

  1. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors.

Maiko KawasakiDepartment of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo, 113-8657, Japan.
Yuta KideraDepartment of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo, 113-8657, Japan.
Ryusei GodaDepartment of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo, 113-8657, Japan.
Chiaki TaketaniDepartment of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo, 113-8657, Japan.
Misato IdeDepartment of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo, 113-8657, Japan.
Wataru FujiiDepartment of Veterinary Medical Sciences, Graduate School of Agricultural and Life Sciences, The University of Tokyo, Tokyo, 113-8657, Japan.
Tomoya NakagitaDepartment of Agricultural Chemistry, School of Agriculture, Meiji University, 1-1-1, Higashimita, Kawasaki, 214-8571, Kanagawa, Japan.
Takumi MisakaDepartment of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo, 113-8657, Japan. amisaka@g.ecc.u-tokyo.ac.jp.

Funding

Japan Society for the Promotion of Science JP16H04918, JP19H02907, JP22H02282, JP22K19128, and JP23K23549
6 · The paper itself

Abstract

The heterodimeric G-protein-coupled receptors T1R2/T1R3 and T1R1/T1R3 have been identified as sweet and umami taste receptors, respectively, and both of these receptors share the T1R3 subunit. Previous research has indirectly indicated functional differences in the T1R3 subunit between the receptors. In this study, a comparative analysis was conducted on the responses of these receptors to substances acting on T1R3, standardizing the response measurement conditions for both. The results revealed significant differences in the modulatory effects of negative allosteric modulators (NAMs) and positive allosteric modulators (PAMs), that act on the transmembrane region of T1R3. Notably, (±)-lactisole, (±)-2,4-DP, and clofibric acid, which are sweet taste receptor inhibitors, also function as umami taste receptor inhibitors, albeit at concentrations approximately 6-10 times greater than those required for sweet taste inhibition. Additionally, cyclamate and NHDC, which are ago-PAMs of sweet taste receptors, did not activate the umami taste receptor at any concentration that significantly elicited sweet taste receptor responses. These results suggest that the binding modes of the substances to the T1R3 subunit of the sweet taste receptor and umami taste receptor are not entirely identical. The difference in the heterodimeric partners to T1R3 may account for their distinct modulation patterns of receptor function.

Indexed as

Receptors, G-Protein-CoupledTasteAllosteric RegulationBenzene DerivativesHEK293 CellsHumansProtein SubunitsBenzene DerivativeslactisoleProtein SubunitsReceptors, G-Protein-Coupledtaste receptors, type 1Negative allosteric modulator (NAM)Positive allosteric modulator (PAM)SweetTasteTaste receptorUmami

Identifiers

PMID40715293
PMCPMC12296726

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