TAS1R3

The protein encoded by the TAS1R3 gene is a G protein-coupled receptor with seven trans-membrane domains and is a component of the heterodimeric amino acid taste receptor TAS1R1+3 and sweet taste receptor TAS1R2+3. This receptor is formed as a protein dimer with either TAS1R1 or TAS1R2.{{cite journal | vauthors = Nelson G, Hoon MA, Chandrashekar J, Zhang Y, Ryba NJ, Zuker CS | title = Mammalian sweet taste receptors | journal = Cell | volume = 106 | issue = 3 | pages = 381–390 | year = 2001 | pmid = 11509186 | doi = 10.1016/S0092-8674(01)00451-2 | s2cid = 11886074 | doi-access = free }}

Experiments have also shown that a homo-dimer of TAS1R3 is also sensitive to natural sugar substances. This has been hypothesized as the mechanism by which sugar substitutes do not have the same taste qualities as natural sugars.{{cite journal | vauthors = Zhao GQ, Zhang Y, Hoon MA, Chandrashekar J, Erlenbach I, Ryba NJ, Zuker CS | title = The receptors for mammalian sweet and umami taste | journal = Cell | volume = 115 | issue = 3 | pages = 255–266 | year = 2003 | pmid = 14636554 | doi = 10.1016/S0092-8674(03)00844-4 | s2cid = 11773362 | doi-access = free }}{{cite journal | vauthors = Yousif RH, Wahab HA, Shameli K, Khairudin NB | title = Exploring the Molecular Interactions between Neoculin and the Human Sweet Taste Receptors through Computational Approaches. | journal = Sains Malaysiana | date = March 2020 | volume = 49 | issue = 3 | pages = 517-525 | doi = 10.17576/jsm-2020-4903-06 | url = http://eprints.utm.my/93942/1/NurulbahiyahAhmadKhairudin2020_ExploringtheMolecularInteractionsbetweenNeoculinandtheHuman.pdf }}

APA

The G protein-coupled receptors for sweet and umami taste are formed by dimers of the TAS1R proteins.

The TAS1R1+3 taste receptor is sensitive to the glutamate in monosodium glutamate (MSG) as well as the synergistic taste-enhancer molecules inosine monophosphate (IMP) and guanosine monophosphate (GMP). These taste-enhancer molecules are unable to activate the receptor alone, but are rather used to enhance receptor responses many to L-amino acids.{{cite journal | vauthors = Nelson G, Chandrashekar J, Hoon MA, Feng L, Zhao G, Ryba NJ, Zuker CS | title = An amino-acid taste receptor | journal = Nature | volume = 416 | issue = 6877 | pages = 199–202 | year = 2002 | pmid = 11894099 | doi = 10.1038/nature726 | bibcode = 2002Natur.416..199N | s2cid = 1730089 }} The TAS1R2+3 receptor has been shown to respond to natural sugars sucrose and fructose, and artificial sweeteners saccharin, acesulfame potassium, dulcin, guanidinoacetic acid.

TAS1R2 and TAS1R1 receptors have been shown to bind to G proteins, most often the gustducin Gα subunit, although a gustducin knock-out has shown small residual activity. TAS1R2 and TAS1R1 have also been shown to activate Gαo and Gαi protein subunits.{{cite journal | vauthors = Sainz E, Cavenagh MM, LopezJimenez ND, Gutierrez JC, Battey JF, Northup JK, Sullivan SL | title = The G-protein coupling properties of the human sweet and amino acid taste receptors | journal = Developmental Neurobiology | volume = 67 | issue = 7 | pages = 948–959 | year = 2007 | pmid = 17506496 | doi = 10.1002/dneu.20403 | s2cid = 29736077 }} This suggests that TAS1R1 and TAS1R2 are G protein-coupled receptors that inhibit adenylyl cyclases to decrease cyclic guanosine monophosphate (cGMP) levels in taste receptors.{{cite journal | vauthors = Abaffy T, Trubey KR, Chaudhari N | title = Adenylyl cyclase expression and modulation of cAMP in rat taste cells | journal = American Journal of Physiology. Cell Physiology | volume = 284 | issue = 6 | pages = C1420–C1428 | year = 2003 | pmid = 12606315 | doi = 10.1152/ajpcell.00556.2002 | s2cid = 2704640 }} The TAS1R3 protein, however, has been shown in vitro to couple with Gα subunits at a much lower rate than the other TAS1R proteins. While the protein structures of the TAS1R proteins are similar, this experiment shows that the G protein-coupling properties of TAS1R3 may be less important in the transduction of taste signals than the TAS1R1 and TAS1R2 proteins.

TAS1R1+3 expressing cells are found in fungiform papillae at the tip and edges of the tongue and palate taste receptor cells in the roof of the mouth. These cells are shown to synapse upon the chorda tympani nerves to send their signals to the brain. TAS1R2+3 expressing cells are found in circumvallate papillae and foliate papillae near the back of the tongue and palate taste receptor cells in the roof of the mouth. These cells are shown to synapse upon the glossopharyngeal nerves to send their signals to the brain.{{cite journal | vauthors = Beamis JF, Shapshay SM, Setzer S, Dumon JF | title = Teaching models for Nd:YAG laser bronchoscopy | journal = Chest | volume = 95 | issue = 6 | pages = 1316–1318 | year = 1989 | pmid = 2721271 | doi = 10.1378/chest.95.6.1316 | doi-access = free }}{{cite journal | vauthors = Danilova V, Hellekant G | title = Comparison of the responses of the chorda tympani and glossopharyngeal nerves to taste stimuli in C57BL/6J mice | journal = BMC Neuroscience | volume = 4 | pages = 5–6 | year = 2003 | pmid = 12617752 | pmc = 153500 | doi = 10.1186/1471-2202-4-5 | doi-access = free }} TAS1R and TAS2R (bitter) channels are not expressed together in any taste buds.

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{{refend}}

• [https://www.genecards.org/cgi-bin/carddisp.pl?gene=TAS1R3 TAS1R3 Gene]
• [http://omim.org/entry/605865 TASTE RECEPTOR TYPE 1, MEMBER 3; TAS1R3]

{{G protein-coupled receptors|g3}}

{{NLM content}}

Category:Human taste receptors