title: ANO2 is the cilial calcium-activated chloride channel that may mediate olfactory amplification.
abstract: For vertebrate olfactory signal transduction, a calcium-activated chloride conductance serves as a major amplification step. However, the molecular identity of the olfactory calcium-activated chloride channel (CaCC) is unknown. Here we report a proteomic screen for cilial membrane proteins of mouse olfactory sensory neurons (OSNs) that identified all the known olfactory transduction components as well as Anoctamin 2 (ANO2). Ano2 transcripts were expressed specifically in OSNs in the olfactory epithelium, and ANO2::EGFP fusion protein localized to the OSN cilia when expressed in vivo using an adenoviral vector. Patch-clamp analysis revealed that ANO2, when expressed in HEK-293 cells, forms a CaCC and exhibits channel properties closely resembling the native olfactory CaCC. Considering these findings together, we propose that ANO2 constitutes the olfactory calcium-activated chloride channel.
authors: Department of Biology, The Johns Hopkins University School of Medicine, Baltimore, MD 21218, USA.
authors: Aaron B
authors: AB
authors: Stephan
authors: Eleen Y
authors: EY
authors: Shum
authors: Sarah
authors: S
authors: Hirsh
authors: Katherine D
authors: KD
authors: Cygnar
authors: Johannes
authors: J
authors: Reisert
authors: Haiqing
authors: H
authors: Zhao
mesh_terms: D000818:Animals; D000075368:Anoctamins; D002460:Cell Line; D018118:Chloride Channels / Q000378:metabolism*; D002923:Cilia / Q000378:metabolism; D006801:Humans; D008565:Membrane Proteins / Q000378:metabolism*; D051379:Mice; D018034:Olfactory Receptor Neurons / Q000378:metabolism; D018408:Patch-Clamp Techniques; D040901:Proteomics; D015398:Signal Transduction / Q000502:physiology*; D012903:Smell / Q000502:physiology*
chemical_list: C532161:ANO2 protein, mouse; D000075368:Anoctamins; D018118:Chloride Channels; D008565:Membrane Proteins