Abstract
The detection of odorants with high sensitivity and specificity utilizes specialized transduction proteins that may be assembled into complexes to afford enhanced speed and efficiency in olfactory neurons. We have used a differential cDNA screening technique to identify novel gene products that display restricted expression within the olfactory epithelium. Here we report the characterization of an olfactory neuronal protein, SLP3, which shares extensive homology with the stomatin family of membrane proteins. Other stomatin family members have been implicated in specific interactions with ion channels and G protein-coupled receptors. The pattern of SLP3 mRNA expression during embryonic development and the subcellular localization of the SLP3 protein in mature olfactory neurons observed here is consistent with a specific role for this protein in the assembly, translocation, or function of the odorant transduction complex in olfactory neurons.
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