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Department of Pharmacology, University of Washington, Seattle, Washington 98195-7280, USA.
Gene disruption studies have shown that the Ca(2+)-stimulated adenylyl cyclases, AC1 and AC8, are critical for some forms of synaptic plasticity, including long-term potentiation as well as long-term memory formation (LTM). It is hypothesized that these enzymes are required for LTM to support the increased expression of a family of genes regulated through the cAMP/Ca(2+) response element-binding protein/cAMP response element transcriptional pathway. In contrast to AC1 and AC8, AC3 is a Ca(2+)-inhibited adenylyl cyclase that plays an essential role in olfactory signal transduction. Coupling of odorant receptors to AC3 stimulates cAMP transients that function as the major second messenger for olfactory signaling. These cAMP transients are caused, at least in part, by Ca(2+) inhibition of AC3, which is mediated through calmodulin-dependent protein kinase II. The unique structure and regulatory properties of these adenylyl cyclases make them attractive drug target sites for modulation of a number of physiological processes including memory formation and olfaction.
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