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- Title
Gγ13 colocalizes with gustducin in taste receptor cells and mediates IP<sub>3</sub> responses to bitter denatonium.
- Authors
Huang, Liquan; Shanker, Y. Gopi; Dubauskaite, Jolanta; Zheng, Jenny Z.; Yan, Wentao; Rosenzweig, Sophia; Spielman, Andrew I.; Max, Marianna; Margolskee, Robert F.
- Abstract
Gustducin is a transducin-like G protein selectively expressed in taste receptor cells. The α subunit of gustducin (α-gustducin) is critical for transduction of responses to bitter or sweet compounds. We identified a G-protein γ subunit (Gγ13) that colocalized with α-gustducin in taste receptor cells. Of 19 α-gustducin/Gγ13-positive taste receptor cells profiled, all expressed the G protein β3 subunit (Gβ3); ∼80% also expressed Gβ1. Gustducin heterotrimers (α-gustducin/Gβ1/Gγ13) were activated by taste cell membranes plus bitter denatonium. Antibodies against Gγ13 blocked the denatoniuminduced increase of inositol trisphosphate (IP[sub 3]) in taste tissue. We conclude that gustducin heterotrimers transduce responses to bitter and sweet compounds via α-gustducin's regulation of phosphodiesterase (PDE) and Gβγ's activation of phospholipase C (PLC).
- Publication
Nature Neuroscience, 1999, Vol 2, Issue 12, p1055
- ISSN
1097-6256
- Publication type
Academic Journal
- DOI
10.1038/15981