Phosphorylation and inhibition of olfactory adenylyl cyclase by CaM kinase II in neurons: A mechanism for attenuation of olfactory signals

Jia Wei, Allan Z. Zhao, Guy C.K. Chan, Lauren P. Baker, Soren Impey, Joseph A. Beavo, Daniel R. Storm

Research output: Contribution to journalArticle

142 Scopus citations

Abstract

Acute desensitization of olfactory signaling is a critical property of the olfactory system that allows animals to detect and respond to odorants. Correspondingly, an important feature of odorant-stimulated cAMP increases is their transient nature, a phenomenon that may be attributable to the unique regulatory properties of the olfactory adenylyl cyclase (AC3). AC3 is stimulated by receptor activation and inhibited by Ca2+ through Ca2+/calmodulin kinase II (CaMKII) phosphorylation at Ser-1076. Since odorant-stimulated cAMP increases are accompanied by elevated intracellular Ca2+, CaMKII inhibition of AC3 may contribute to termination of olfactory signaling. To test this hypothesis, we generated a polyclonal antibody specific for AC3 phosphorylated at Ser-1076. A brief exposure of mouse olfactory cilia or primary olfactory neurons to odorants stimulated phosphorylation of AC3 at Ser-1076. This phosphorylation was blocked by inhibitors of CaMKII, which also ablated cAMP decreases associated with odorant-stimulated cAMP transients. These data define a novel mechanism for termination of olfactory signaling that may be important in olfactory responses.

Original languageEnglish (US)
Pages (from-to)495-504
Number of pages10
JournalNeuron
Volume21
Issue number3
DOIs
StatePublished - Sep 1998

ASJC Scopus subject areas

  • Neuroscience(all)

Fingerprint Dive into the research topics of 'Phosphorylation and inhibition of olfactory adenylyl cyclase by CaM kinase II in neurons: A mechanism for attenuation of olfactory signals'. Together they form a unique fingerprint.

  • Cite this