Oligomerization of G-protein-coupled transmitter receptors

Nat Rev Neurosci. 2001 Apr;2(4):274-86. doi: 10.1038/35067575.


Examples of G-protein-coupled receptors that can be biochemically detected in homo- or heteromeric complexes are emerging at an accelerated rate. Biophysical approaches have confirmed the existence of several such complexes in living cells and there is strong evidence to support the idea that dimerization is important in different aspects of receptor biogenesis and function. While the existence of G-protein-coupled-receptor homodimers raises fundamental questions about the molecular mechanisms involved in transmitter recognition and signal transduction, the formation of heterodimers raises fascinating combinatorial possibilities that could underlie an unexpected level of pharmacological diversity, and contribute to cross-talk regulation between transmission systems. Because G-protein-coupled receptors are major pharmacological targets, the existence of dimers could have important implications for the development and screening of new drugs. Here, we review the evidence supporting the existence of G-protein-coupled-receptor dimerization and discuss its functional importance.

Publication types

  • Review

MeSH terms

  • Biological Transport
  • Dimerization
  • Energy Transfer
  • Fluorescence
  • Genetic Complementation Test
  • Heterotrimeric GTP-Binding Proteins / metabolism*
  • Light
  • Molecular Chaperones / metabolism
  • Precipitin Tests
  • Receptor Aggregation
  • Receptors, Dopamine D1 / metabolism
  • Receptors, Dopamine D5
  • Receptors, GABA-A / metabolism
  • Receptors, Neurotransmitter / metabolism*
  • Signal Transduction


  • Molecular Chaperones
  • Receptors, Dopamine D1
  • Receptors, GABA-A
  • Receptors, Neurotransmitter
  • Receptors, Dopamine D5
  • Heterotrimeric GTP-Binding Proteins