Tonic activity of Galpha-gustducin regulates taste cell responsivity.

Tod R. Clapp, Kristina R. Trubey, Aurelie Vandenbeuch, Leslie M. Stone, Robert F. Margolskee, Nirupa Chaudhari, Sue C. Kinnamon

Research output: Contribution to journalArticlepeer-review

59 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)3783-3787
Number of pages5
JournalFEBS letters
Issue number27
StatePublished - Nov 12 2008
Externally publishedYes


  • Calcium signaling
  • Phosphodiesterase
  • Protein kinase A
  • Taste transduction

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Cell Biology
  • Genetics
  • Molecular Biology
  • Structural Biology


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