A metabotropic glutamate receptor variant functions as a taste receptor

Nat Neurosci. 2000 Feb;3(2):113-9. doi: 10.1038/72053.

Abstract

Sensory transduction for many taste stimuli such as sugars, some bitter compounds and amino acids is thought to be mediated via G protein-coupled receptors (GPCRs), although no such receptors that respond to taste stimuli are yet identified. Monosodium L-glutamate (L-MSG), a natural component of many foods, is an important gustatory stimulus believed to signal dietary protein. We describe a GPCR cloned from rat taste buds and functionally expressed in CHO cells. The receptor couples negatively to a cAMP cascade and shows an unusual concentration-response relationship. The similarity of its properties to MSG taste suggests that this receptor is a taste receptor for glutamate.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Brain / metabolism
  • CHO Cells
  • Chemoreceptor Cells / metabolism*
  • Cloning, Molecular
  • Colforsin / pharmacology
  • Cricetinae
  • Cyclic AMP / metabolism
  • DNA, Complementary / genetics
  • Dose-Response Relationship, Drug
  • GTP-Binding Proteins / metabolism
  • Glutamic Acid / metabolism*
  • Glutamic Acid / pharmacology
  • Molecular Sequence Data
  • Organ Specificity
  • Polymerase Chain Reaction
  • Propionates / pharmacology
  • Protein Isoforms / genetics
  • Protein Isoforms / metabolism*
  • RNA, Messenger / biosynthesis
  • Rats
  • Receptors, Metabotropic Glutamate / genetics
  • Receptors, Metabotropic Glutamate / metabolism*
  • Taste / physiology*
  • Taste Buds / metabolism*
  • Transfection

Substances

  • 2-amino-4-phosphono-propinate
  • DNA, Complementary
  • Propionates
  • Protein Isoforms
  • RNA, Messenger
  • Receptors, Metabotropic Glutamate
  • Colforsin
  • Glutamic Acid
  • Cyclic AMP
  • GTP-Binding Proteins
  • metabotropic glutamate receptor 4