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Vol. 63, Issue 3, 463-468, March 2003
Department of Pharmacology, University of Washington, Seattle,
Washington
Gene disruption studies have shown that the Ca2+-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/Ca2+ response
element-binding protein/cAMP response element transcriptional pathway.
In contrast to AC1 and AC8, AC3 is a Ca2+-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
Ca2+ 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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