Co-expression of anoctamins in cilia of olfactory sensory neurons

• Published in: Chemical senses 2015-02, Vol.40 (2), p.73-87
• Main Authors: Henkel, Bastian, Drose, Daniela R, Ackels, Tobias, Oberland, Sonja, Spehr, Marc, Neuhaus, Eva M
• Format: Article
• Language: English
• Subjects: Animals; Anoctamins; Chloride Channels - genetics; Chloride Channels - metabolism; Cilia - metabolism; Cyclic Nucleotide-Gated Cation Channels - metabolism; Gene Expression Regulation; HEK293 Cells; Humans; Mice, Inbred C57BL; Olfactory Mucosa - cytology; Olfactory Mucosa - metabolism; Olfactory Receptor Neurons - metabolism; Phospholipid Transfer Proteins - genetics; Phospholipid Transfer Proteins - metabolism; Protein Multimerization; Recombinant Proteins - genetics; Recombinant Proteins - metabolism; Sensory Receptor Cells - metabolism; Signal Transduction
• ISSN: 0379-864X; 1464-3553
• DOI: 10.1093/chemse/bju061

Vertebrates can sense and identify a vast array of chemical cues. The molecular machinery involved in chemodetection and transduction is expressed within the cilia of olfactory sensory neurons. Currently, there is only limited information available on the distribution and density of individual signaling components within the ciliary compartment. Using super-resolution microscopy, we show here that cyclic-nucleotide-gated channels and calcium-activated chloride channels of the anoctamin family are localized to discrete microdomains in the ciliary membrane. In addition to ANO2, a second anoctamin, ANO6, also localizes to ciliary microdomains. This observation, together with the fact that ANO6 and ANO2 co-localize, indicates a role for ANO6 in olfactory signaling. We show that both ANO2 and ANO6 can form heteromultimers and that this heteromerization alters the recombinant channels' physiological properties. Thus, we provide evidence for interaction of ANO2 and ANO6 in olfactory cilia, with possible physiological relevance for olfactory signaling.