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Sci. Signal., 10 April 2012
Vol. 5, Issue 219, p. ra29
[DOI: 10.1126/scisignal.2002299]


Editor's Summary

Bound to Signal in Close Quarters
Interplay between the calcium and the cyclic adenosine monophosphate (cAMP) signaling pathways is crucial to numerous physiological events. Although membrane-bound calcium-sensitive adenylyl cyclases (ACs) are sensitive to submicromolar concentrations of calcium in vitro, in cells they are highly selective in responding to store-operated calcium (SOC) entry rather than to calcium released from intracellular stores or entering the cell through ionophores. Here, Willoughby et al. used a combination of live-cell imaging techniques and biochemical approaches to resolve this conundrum and showed that AC8, which is stimulated by calcium-bound calmodulin, forms a direct protein-protein interaction with Orai1, the pore-forming component of the channel that mediates SOC entry. The existence of AC8 in a complex with SOC channels provides a mechanism for the compartmentalized regulation of cAMP signaling by specific subcellular calcium signals.

Citation: D. Willoughby, K. L. Everett, M. L. Halls, J. Pacheco, P. Skroblin, L. Vaca, E. Klussmann, D. M. F. Cooper, Direct Binding Between Orai1 and AC8 Mediates Dynamic Interplay Between Ca2+ and cAMP Signaling. Sci. Signal. 5, ra29 (2012).

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A key phosphorylation site in AC8 mediates regulation of Ca2+-dependent cAMP dynamics by an AC8-AKAP79-PKA signalling complex.
D. Willoughby, M. L. Halls, K. L. Everett, A. Ciruela, P. Skroblin, E. Klussmann, and D. M. F. Cooper (2012)
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