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Coding of sweet, bitter, and umami tastes: different receptor cells sharing similar signaling pathways.

Mammals can taste a wide repertoire of chemosensory stimuli. Two unrelated families of receptors (T1Rs and T2Rs) mediate responses to sweet, amino acids, and bitter compounds. Here, we demonstrate that knockouts of TRPM5, a taste TRP ion channel, or PLCbeta2, a phospholipase C selectively expressed in taste tissue, abolish sweet, amino acid, and bitter taste reception, but do not impact sour or salty tastes. Therefore, despite relying on different receptors, sweet, amino acid, and bitter transduction converge on common signaling molecules. Using PLCbeta2 taste-blind animals, we then examined a fundamental question in taste perception: how taste modalities are encoded at the cellular level. Mice engineered to rescue PLCbeta2 function exclusively in bitter-receptor expressing cells respond normally to bitter tastants but do not taste sweet or amino acid stimuli. Thus, bitter is encoded independently of sweet and amino acids, and taste receptor cells are not broadly tuned across these modalities.

Pubmed ID: 12581520


  • Zhang Y
  • Hoon MA
  • Chandrashekar J
  • Mueller KL
  • Cook B
  • Wu D
  • Zuker CS
  • Ryba NJ



Publication Data

February 7, 2003

Associated Grants


Mesh Terms

  • Action Potentials
  • Animals
  • Cell Membrane
  • Cells, Cultured
  • Citric Acid
  • Female
  • GTP-Binding Proteins
  • Glutamic Acid
  • Isoenzymes
  • Male
  • Membrane Proteins
  • Mice
  • Mice, Knockout
  • Neurons, Afferent
  • Phospholipase C beta
  • Quinine
  • Receptors, Cell Surface
  • Sensory Receptor Cells
  • Signal Transduction
  • Sucrose
  • TRPM Cation Channels
  • Taste
  • Taste Buds
  • Type C Phospholipases