Coupling of bitter receptor to phosphodiesterase through transducin in taste receptor cells.

Abstract:

: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.

journal_name

Nature

journal_title

Nature

authors

Ruiz-Avila L,McLaughlin SK,Wildman D,McKinnon PJ,Robichon A,Spickofsky N,Margolskee RF

doi

10.1038/376080a0

subject

Has Abstract

pub_date

1995-07-06 00:00:00

pages

80-5

issue

6535

eissn

0028-0836

issn

1476-4687

journal_volume

376

pub_type

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