【摘 要】
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In an attempt to elucidate the molecular basis of vertebrate olfactory signal transduction, we have recently conducted a proteomic screen for cilial membran
【机 构】
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Department of Biology,The Johns Hopkins University,3400 N Charles Street,Baltimore,MD 21212
【出 处】
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The 3rd Ion Channel Conference: Ion channels-Structure, Func
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In an attempt to elucidate the molecular basis of vertebrate olfactory signal transduction, we have recently conducted a proteomic screen for cilial membrane proteins of mouse olfactory sensory neurons (OSNs).This screen led to identify the long-sought olfactory Ca2+-activated Clchannel (CaCC) Anoctamin 2 (ANO2) (Stephan, et al., 2009), which mediates amplification of olfactory signal transduction.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.We have also found several splicing variants of Ano2 transcripts, which encode proteins with distinct trafficking properties when expressed in HEK-293 cells.
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