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

Liquan Huang, Y. Gopi Shanker, Jolanta Dubauskaite, Jenny Z. Zheng, Wentao Yan, Sophia Rosenweig, Andrew I. Spielman, Marianna Max, Robert F. Margolskee

Research output: Contribution to journalArticlepeer-review


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 denatonium-induced increase of inositol trisphosphate (IP3) 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).

Original languageEnglish (US)
Pages (from-to)1055-1062
Number of pages8
JournalNature Neuroscience
Issue number12
StatePublished - Jul 1 1999

ASJC Scopus subject areas

  • Neuroscience(all)


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