Phosphorylation and inhibition of olfactory adenylyl cyclase by CaM kinase II in Neurons: a mechanism for attenuation of olfactory signals
| Autor: | J, Wei, A Z, Zhao, G C, Chan, L P, Baker, S, Impey, J A, Beavo, D R, Storm |
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| Rok vydání: | 1998 |
| Předmět: |
Male
Neurons Models Biological Peptide Fragments Mice Inbred C57BL Mice Animals Newborn Olfactory Mucosa Adenylyl Cyclase Inhibitors Calcium-Calmodulin-Dependent Protein Kinases Odorants Cyclic AMP Serine Animals Cilia Enzyme Inhibitors Phosphorylation Calcium-Calmodulin-Dependent Protein Kinase Type 2 Cells Cultured Adenylyl Cyclases Signal Transduction |
| Zdroj: | Neuron. 21(3) |
| ISSN: | 0896-6273 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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