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Biochem Biophys Res Commun. 2010 Jan 15;391(3):1379-84. doi: 10.1016/j.bbrc.2009.12.068. Epub 2009 Dec 22.

Distinct ONE-GC transduction modes and motifs of the odorants: Uroguanylin and CO(2).

Author information

1
Research Divisions of Biochemistry and Molecular Biology, The Unit of Regulatory and Molecular Biology, Salus University, Elkins Park, PA 19027, USA. tduda@salus.edu

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 CO(2). 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, CO(2) transduction mechanism is Ca(2+)-independent. (2) CO(2) transduction site, like that of uroguanylin-neurocalcin delta, resides in the core catalytic domain, aa 880-1028, of ONE-GC. (3) The site, however, does not overlap the signature neurocalcin delta signal transduction domain, (908)LSEPIE(913). Finally, (4) this study negates the prevailing concept that CO(2) 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.

PMID:
20026308
PMCID:
PMC2839448
DOI:
10.1016/j.bbrc.2009.12.068
[Indexed for MEDLINE]
Free PMC Article

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