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Oligomerization of TAS2R bitter taste receptors

Christina Kuhn1, Bernd Bufe, Claudia Batram

  • 1Department of Molecular Genetics, German Institute of Human Nutrition Potsdam-Rehbruecke, Arthur-Scheunert-Allee 114-116, Nuthetal 14558, Germany.

Chemical Senses
|March 10, 2010
PubMed

Insights

Bitter taste receptors (TAS2Rs) can form physical pairs (oligomers) with each other. However, this study found no clear functional changes resulting from these bitter receptor interactions.

Area of Science:

  • Molecular biology
  • Sensory science
  • G protein-coupled receptors

Background:

  • Taste receptor type 2 (TAS2R) proteins mediate human bitter taste perception.
  • Coexpression of TAS2Rs in taste cells suggests potential for receptor-receptor interactions.

Purpose of the Study:

  • To investigate if TAS2Rs form oligomers (homomers or heteromers).
  • To determine the functional consequences of TAS2R hetero-oligomerization.

Main Methods:

  • Coimmunoprecipitation assays to detect physical interactions.
  • Bioluminescence resonance energy transfer (BRET) to analyze all binary TAS2R combinations.
  • Screening coexpressed receptors with 104 tastants.

Main Results:

  • Coimmunoprecipitation confirmed physical interactions between TAS2Rs.
  • BRET analysis revealed that most TAS2R pairs form homomers and heteromers.
  • No heteromer-specific agonists were identified.
  • Hetero-oligomerization did not obviously affect receptor localization or pharmacology.

Conclusions:

  • TAS2R bitter taste receptors do physically oligomerize.
  • The functional impact of TAS2R hetero-oligomerization remains unclear based on current findings.

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