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The Journal of Neuroscience, August 13, 2003, 23(19):7376-7380
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Functional Interaction between T2R Taste Receptors and G-Protein  Subunits Expressed in Taste Receptor Cells
Takashi Ueda,1
Shinya Ugawa,1
Hisao Yamamura,1,2
Yuji Imaizumi,2 and
Shoichi Shimada1
1Department of Molecular Morphology, Graduate
School of Medical Sciences, Nagoya City University, and
2Department of Molecular and Cellular Pharmacology,
Graduate School of Pharmaceutical Sciences, Nagoya City University, Nagoya
467-8601, Japan
Bitter taste perception is a conserved chemical sense against the ingestion
of poisonous substances in mammals. A multigene family of G-protein-coupled
receptors, T2R (so-called TAS2R or TRB) receptors and a G-protein 
subunit (G), gustducin, are believed to be key molecules for its
perception, but little is known about the molecular basis for its interaction.
Here, we use a heterologous expression system to determine a specific domain
of gustducin necessary for T2R coupling. Two chimeric G16 proteins
harboring 37 and 44 gustducin-specific sequences at their C termini
(G16/gust37 and G16/gust44) responded to different T2R receptors with known
ligands, but G16/gust 23, G16/gust11, and G16/gust5 did not. The former two
chimeras contained a predicted 6 sheet, an5 helix, and an extreme
C terminus of gustducin, and all the domains were indispensable to the
expression of T2R activity. We also expressed G16 protein chimeras with the
corresponding domain from other Gi proteins, cone-transducin
(Gt2), Gi2, and Gz (G16/t2, G16/i2, and G16/z). As a
result, G16/t2 and G16/i2 produced specific responses of T2Rs, but G16/z did
not. Because Gt2 and Gi2 are expressed in the taste receptor
cells, these G-protein i subunits may also be involved in bitter taste
perception via T2R receptors. The present G16-based chimeras could be
useful tools to analyze the functions of many orphan G-protein-coupled taste
receptors.
Key words: bitter taste; T2R receptor; G-protein subunit; gustducin; G chimera; calcium imaging
Received May. 6, 2003;
revised Jun. 9, 2003;
accepted Jun. 18, 2003.
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