Odorant receptor heterodimerization in the olfactory system of Drosophila melanogaster

Nat Neurosci. 2005 Jan;8(1):15-7. doi: 10.1038/nn1371. Epub 2004 Dec 12.


Despite increasing knowledge about dimerization of G-protein-coupled receptors, nothing is known about dimerization in the largest subfamily, odorant receptors. Using a combination of biochemical and electrophysiological approaches, we demonstrate here that odorant receptors can dimerize. DOR83b, an odorant receptor that is ubiquitously expressed in olfactory neurons from Drosophila melanogaster and highly conserved among insect species, forms heterodimeric complexes with other odorant-receptor proteins, which strongly increases their functionality.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cell Line
  • Dimerization
  • Drosophila Proteins / genetics
  • Drosophila Proteins / metabolism*
  • Drosophila melanogaster / metabolism*
  • Humans
  • Olfactory Pathways / metabolism*
  • RNA Interference
  • Receptors, Odorant / genetics
  • Receptors, Odorant / metabolism*
  • Transfection


  • Drosophila Proteins
  • OR22a protein, Drosophila
  • OR43b protein, Drosophila
  • Orco protein, Drosophila
  • Receptors, Odorant