Gustducin and its role in taste

J Dent Res. 1998 Apr;77(4):539-44. doi: 10.1177/00220345980770040601.


The mechanisms responsible for taste signal transductions are very complex. A key molecule, alpha-gustducin, a primarily taste-specific G protein alpha-subunit, was discovered in 1992 and was later found to be involved in both bitter and sweet taste transduction. A proposed mechanism for alpha-gustducin involves coupling specific cell-surface receptors with a cyclic nucleotide phosphodiesterase which would open a cyclic nucleotide-suppressible cation channel leading to influx of calcium, and ultimately leading to release of neurotransmitter. Although "knock-out" animals deficient in the alpha-gustducin gene clearly demonstrate that gustducin is an essential molecule for tasting certain bitter and sweet compounds, the precise role of alpha-gustducin in bitter and sweet taste is presently unclear. Indeed, there are several other signaling mechanisms in sweet and bitter taste, apparently unrelated to alpha-gustducin, that increase cyclic AMP or inositol 1,4,5 trisphosphate. Thus, proposed models for alpha-gustducin and those found by other laboratories may be parallel and interdependent.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Animals
  • Calcium Channels / physiology
  • Cyclic AMP / physiology
  • GTP-Binding Proteins / classification
  • Humans
  • Inositol 1,4,5-Trisphosphate / physiology
  • Neurotransmitter Agents / physiology
  • Nucleotides / physiology
  • Phosphoric Diester Hydrolases / physiology
  • Receptors, Cell Surface / physiology
  • Signal Transduction / physiology
  • Taste / physiology*
  • Transducin / genetics
  • Transducin / physiology*


  • Calcium Channels
  • Neurotransmitter Agents
  • Nucleotides
  • Receptors, Cell Surface
  • gustducin
  • Inositol 1,4,5-Trisphosphate
  • Cyclic AMP
  • Phosphoric Diester Hydrolases
  • GTP-Binding Proteins
  • Transducin