Tonic activity of Galpha-gustducin regulates taste cell responsivity |
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Authors: | Clapp Tod R Trubey Kristina R Vandenbeuch Aurelie Stone Leslie M Margolskee Robert F Chaudhari Nirupa Kinnamon Sue C |
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Affiliation: | a Department of Biomedical Sciences, Colorado State University, Fort Collins, CO 80523, United States b Rocky Mountain Taste and Smell Center, University of Colorado Denver, Aurora, CO 80045, United States c Department of Physiology and Biophysics, University of Miami Miller School of Medicine, Miami, FL 33136, United States d Program in Neurosciences, University of Miami Miller School of Medicine, Miami, FL 33136, United States e Department of Neuroscience, Mount Sinai School of Medicine, New York, NY 10029, United States |
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Abstract: | The taste-selective G protein, α-gustducin (α-gus) is homologous to α-transducin and activates phosphodiesterase (PDE) in vitro. α-Gus-knockout mice are compromized to bitter, sweet and umami taste stimuli, suggesting a central role in taste transduction. Here, we suggest a different role for Gα-gus. In taste buds of α-gus-knockout mice, basal (unstimulated) cAMP levels are high compared to those of wild-type mice. Further, H-89, a cAMP-dependent protein kinase inhibitor, dramatically unmasks responses to the bitter tastant denatonium in gus-lineage cells of knockout mice. We propose that an important role of α-gus is to maintain cAMP levels tonically low to ensure adequate Ca2+ signaling. |
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Keywords: | CMF, calcium-magnesium free CV, circumvallate GFP, green fluorescent protein GPCR, G protein-coupled receptor Gus, gustducin IP3R3, inositol trisphosphate receptor type III PDE, phosphodiesterase PKA, protein kinase A PKC, protein kinase C PLCβ2, phospholipase C β2 |
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