Local Termination of 3′-5′-Cyclic Adenosine Monophosphate Signals: The Role of A Kinase Anchoring Protein–Tethered Phosphodiesterases


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Abstract

A kinase anchoring proteins (AKAPs) belong to a family of functionally related proteins capable of binding protein kinase A (PKA) and tether it to relevant targets. In this way, AKAPs organize macromolecular complexes to segregate PKA activity and retain signal specificity. In the heart, AKAP–PKA interaction is central to the regulation of cardiac contractility. Phosphodiesterases belong to a large superfamily of enzymes that degrade 3′-5′-cyclic adenosine monophosphate (cAMP). They possess diverse catalytic properties and multiple regulatory mechanisms and control the duration and amplitude of the cAMP signal, including its propagation in space. AKAPs, together with PKA, can also assemble phosphodiesterases thereby providing a means to locally control cAMP dynamics at the level of single macromolecular complexes. This allows for the fine tuning of the cAMP response to the specific demands of the cell.

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