Gγ13 colocalizes with gustducin in taste receptor cells and mediates IP3 responses to bitter denatonium

被引:264
作者
Huang, LQ
Shanker, YG
Dubauskaite, J
Zheng, JZ
Yan, WT
Rosenzweig, S
Spielman, AI
Max, M
Margolskee, RF
机构
[1] NYU, Mt Sinai Sch Med, Howard Hughes Med Inst, New York, NY 10029 USA
[2] NYU, Mt Sinai Sch Med, Dept Physiol & Biophys, New York, NY 10029 USA
[3] NYU, Coll Dent, Div Basic Sci, New York, NY 10010 USA
关键词
D O I
10.1038/15981
中图分类号
Q189 [神经科学];
学科分类号
071006 ;
摘要
Gustducin is a transducin-like G protein selectively expressed in taste receptor cells. The alpha subunit of gustducin (alpha-gustducin) is critical for transduction of responses to bitter or sweet compounds. We identified a G-protein gamma subunit (G gamma 13) that colocalized with alpha-gustducin in taste receptor cells. Of 19 alpha-gustducin/Gy13-positive taste receptor cells profiled, all expressed the G protein beta 3 subunit (G beta 3); similar to 80% also expressed G beta 1. Gustducin heterotrimers (alpha-gustducin/G beta 1/G gamma 13) were activated by taste cell membranes plus bitter denatonium. Antibodies against G gamma 13 blocked the denatonium-induced increase of inositol trisphosphate (IP3) in taste tissue. We conclude that gustducin heterotrimers transduce responses to bitter and sweet compounds via alpha-gustducin's regulation of phosphodiesterase (PDE) and G beta gamma's activation of phospholipase C (PLC).
引用
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页码:1055 / 1062
页数:8
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