A novel G protein alpha-subunit (alpha-gustducin) has been identified and cloned from taste tissue. alpha-Gustducin messenger RNA is expressed in taste buds of all taste papillae (circumvallate, foliate and fungiform); it is not expressed in non-sensory portions of the tongue, nor is it expressed in the other tissues examined. alpha-Gustducin most closely resembles the transducins (the rod and cone photoreceptor G proteins), suggesting that gustducin's role in taste transduction is analogous to that of transducin in light transduction.
The rod and cone transducins are specific G proteins originally thought to be present only in photoreceptor cells of the vertebrate retina. Transducins convert light stimulation of photoreceptor opsins into activation of cyclic GMP phosphodiesterase (reviewed in refs. 5-7). A transducin-like G protein, gustducin, has been identified and cloned from rat taste cells. We report here that rod transducin is also present in vertebrate taste cells, where it specifically activates a phosphodiesterase isolated from taste tissue. Furthermore, the bitter compound denatonium in the presence of taste-cell membranes activates transducin but not Gi. A peptide that competitively inhibits rhodopsin activation of transducin also blocks taste-cell membrane activation of transducin, arguing for the involvement of a seven-transmembrane-helix G-protein-coupled receptor. These results suggest that rod transducin transduces bitter taste by coupling taste receptor(s) to taste-cell phosphodiesterase. Phosphodieterase-mediated degradation of cyclic nucleotides may lead to taste-cell depolarization through the recently identified cyclic-nucleotide-suppressible conductance.
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