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.
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*Note: In the version of this article originally published online, the legend to Figure 1d was printed incorrectly. It should read: (d) Cyclohexanone-induced increase in intracellular Ca2+ in HEK293 cells transfected with DOR43a alone (h) and with DOR43a + DOR83b (i). This error has been corrected in the HTML and print versions of the article.
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We thank J. Gerkrath, W. Grabowski, M. Köper, H. Bartel and K. Farhat for technical assistance and B. Ache for critical reading of the manuscript. This work was supported by grants from the Deutsche Forschungsgemeinschaft to E.M.N. and H.H. (SFB642) and to K.F.S. (STD283/8-1), and by the Max Planck Research School for Chemical Biology (IMPRS-CB).
The authors declare no competing financial interests.
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Neuhaus, E., Gisselmann, G., Zhang, W. et al. Odorant receptor heterodimerization in the olfactory system of Drosophila melanogaster. Nat Neurosci 8, 15–17 (2005) doi:10.1038/nn1371
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