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

doi:10.1016/j.febslet.2008.10.007

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

Physiology & Biophysics

Research output: Contribution to journal › Article

49 Scopus citations

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)
Pages (from-to)	3783-3787
Number of pages	5
Journal	FEBS letters
Volume	582
Issue number	27
DOIs	https://doi.org/10.1016/j.febslet.2008.10.007
State	Published - Nov 12 2008

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Keywords

Calcium signaling
Phosphodiesterase
Protein kinase A
Taste transduction

ASJC Scopus subject areas

Biochemistry
Biophysics
Cell Biology
Genetics
Molecular Biology
Structural Biology

Cite this

Clapp, T. R., Trubey, K. R., Vandenbeuch, A., Stone, L. M., Margolskee, R. F., Chaudhari, N., & Kinnamon, S. C. (2008). Tonic activity of Galpha-gustducin regulates taste cell responsivity. FEBS letters, 582(27), 3783-3787. https://doi.org/10.1016/j.febslet.2008.10.007

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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.",

keywords = "Calcium signaling, Phosphodiesterase, Protein kinase A, Taste transduction",

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AU - Clapp, Tod R.

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AU - Vandenbeuch, Aurelie

AU - Stone, Leslie M.

AU - Margolskee, Robert F.

AU - Chaudhari, Nirupa

AU - Kinnamon, Sue C.

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AB - 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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Access to Document

10.1016/j.febslet.2008.10.007