Interaction between domains of the umami receptor, T1R1 and T1R3

2014 Fiscal Year Final Research Report

• Project/Area Number: 24657120
• Research Category: Grant-in-Aid for Challenging Exploratory Research
• Allocation Type: Multi-year Fund
• Research Field: Molecular biology
• Research Institution: Ishikawa Prefectural University
• Principal Investigator: MITSURU Ebihara 石川県立大学, 生物資源環境学部, 准教授 (80232974)
• Project Period (FY): 2012-04-01 – 2015-03-31
• 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

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.

Free Research Field

分子生物学