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.
Original language | English (US) |
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Pages (from-to) | 3783-3787 |
Number of pages | 5 |
Journal | FEBS letters |
Volume | 582 |
Issue number | 27 |
DOIs | |
State | Published - Nov 12 2008 |
Externally published | Yes |
Keywords
- Calcium signaling
- Phosphodiesterase
- Protein kinase A
- Taste transduction
ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Cell Biology
- Genetics
- Molecular Biology
- Structural Biology