Interaction between domains of the umami receptor, T1R1 and T1R3
| Project/Area Number |
24657120
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| Research Category |
Grant-in-Aid for Challenging Exploratory Research
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| Allocation Type | Multi-year Fund |
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| Research Field |
Molecular biology
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| Research Institution | Ishikawa Prefectural University |
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Principal Investigator |
MITSURU Ebihara 石川県立大学, 生物資源環境学部, 准教授 (80232974)
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| Project Period (FY) |
2012-04-01 – 2015-03-31
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| Project Status |
Completed (Fiscal Year 2014)
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| Budget Amount *help |
¥4,030,000 (Direct Cost: ¥3,100,000、Indirect Cost: ¥930,000)
Fiscal Year 2014: ¥1,040,000 (Direct Cost: ¥800,000、Indirect Cost: ¥240,000)
Fiscal Year 2013: ¥910,000 (Direct Cost: ¥700,000、Indirect Cost: ¥210,000)
Fiscal Year 2012: ¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
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| Keywords | うま味受容体 / タンパク質－タンパク質相互作用 / GPCR / split GFP法 / 味覚受容体 / 相互作用 / ポリロイシン / 膜貫通ドメイン / トリプレットリピート / 膜タンパク質 |
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| Outline of Final Research Achievements |
Umami receptors, T1R1 and T1R3 are known to form heterodimer, but mechanism of interaction between them remain unclear. In this study, interaction between leucine repeat which exist in the first transmembrane domain of T1R1 and T1R3 was analyzed by using split GFP method. It was shown that both of leucine repeats from the first transmembrane domains have a role in T1R1-T1R3 interaction, at least in part. Hybrid molecules constructed from the umami receptor genes of carnivore, herbivore and omnivore animals may reveal which transmembrane domains could be involved in dimerization of T1R1 and T1R3. Furthermore, this interaction may affect function of the umami receptors and perception of umami taste.
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Report
(4 results)
Research Products
(14 results)
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[Presentation] Analysis of protein-protein interaction between transmembrane domains derived from human taste receptor, T1R1 and T1R3.2014
Author(s)
Kato, A., Nishi, K., Domae, H., Mima, H., and Ebihara, M.
Organizer
第37回日本分子生物学会
Place of Presentation
横浜
Year and Date
2014-11-25 – 2014-11-27
Related Report
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