Distinct ONE-GC transduction modes and motifs of the odorants: Uroguanylin and CO2 |
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Authors: | Teresa Duda Rameshwar K Sharma |
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Institution: | Research Divisions of Biochemistry and Molecular Biology, The Unit of Regulatory and Molecular Biology, Salus University, Elkins Park, PA 19027, USA |
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Abstract: | In a subset of the olfactory sensory neurons ONE-GC$ membrane guanylate cyclase is a central component of two odorant-dependent cyclic GMP signaling pathways. These odorants are uroguanylin and CO2. The present study was designed to decipher the biochemical and molecular differences between these two odorant signaling mechanisms. The study shows (1) in contrast to uroguanylin, CO2 transduction mechanism is Ca2+-independent. (2) CO2 transduction site, like that of uroguanylin-neurocalcin δ, resides in the core catalytic domain, aa 880-1028, of ONE-GC. (3) The site, however, does not overlap the signature neurocalcin δ signal transduction domain, 908LSEPIE913. Finally, (4) this study negates the prevailing concept that CO2 uniquely signals ONE-GC activity (Sun et al. 19]; Guo et al. 21]). It demonstrates that it also signals the activation of photoreceptor membrane guanylate cyclase ROS-GC1. These results show an additional new transduction mechanism of the membrane guanylate cyclases and broaden our understanding of the molecular mechanisms by which different odorants using a single guanylate cyclase can regulate diverse cyclic GMP signaling pathways. |
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Keywords: | aa amino acid Catd catalytic domain ONE-GC olfactory neuroepithelial membrane guanylate cyclase ROS-GC rod outer segment membrane guanylate cyclase tm-catd transmembrane linked catalytic domain |
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