Bitter taste transduced by PLC-β2-dependent rise in IP3 and α-gustducin-dependent fall in cyclic nucleotides

Wentao Yan, Gulshan Sunavala, Sophia Rosenzweig, Max Dasso, Joseph G. Brand, Andrew I. Spielman

Research output: Contribution to journalArticlepeer-review


Current evidence points to the existence of multiple processes for bitter taste transduction. Previous work demonstrated involvement of the polyphosphoinositide system and an α-gustducin (Gαgust)-mediated stimulation of phosphodiesterase in bitter taste transduction. Additionally, a taste-enriched G protein γ-subunit, Gγ13, colocalizes with Gαgust and mediates the denatonium-stimulated production of inositol 1,4,5-triphosphate (IP3). Using quench-flow techniques, we show here that the bitter stimuli, denatonium and strychnine, induce rapid (50-100 ms) and transient reductions in cAMP and cGMP and increases in IP3 in murine taste tissue. This decrease of cyclic nucleotides is inhibited by Gαgust antibodies, whereas the increase in IP3 is not affected by antibodies to Gαgust. IP3 production is inhibited by antibodies specific to phospholipase C-β2 (PLC-β2), a PLC isoform known to be activated by Gβγ-subunits. Antibodies to PLC-β3 or to PLC-β4 were without effect. These data suggest a transduction mechanism for bitter taste involving the rapid and transient metabolism of dual second messenger systems, both mediated through a taste cell G protein, likely composed of Gαgust/β/γ13, with both systems being simultaneously activated in the same bitter-sensitive taste receptor cell.

Original languageEnglish (US)
Pages (from-to)C742-C751
JournalAmerican Journal of Physiology - Cell Physiology
Issue number4 49-4
StatePublished - 2001


  • Denatonium
  • Inositol 1,4,5-triphosphate
  • Phospholipase C
  • Rapid kinetics
  • Second messenger
  • Taste receptors
  • Taste transduction

ASJC Scopus subject areas

  • Physiology
  • Cell Biology


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