Journal
MOLECULAR CELL
Volume 23, Issue 6, Pages 925-931Publisher
CELL PRESS
DOI: 10.1016/j.molcel.2006.07.025
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Funding
- NIGMS NIH HHS [R01 GM060419, GM60419, R01 GM048231, R37 GM048231, GM48231, R01 GM060419-07] Funding Source: Medline
- NINDS NIH HHS [F32 NS045513, NS045513] Funding Source: Medline
- Wellcome Trust Funding Source: Medline
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Spatiotemporal organization of cAMP signaling begins with the tight control of second messenger synthesis. In response to agonist stimulation of G protein-coupled receptors, membrane-associated adenylyl cyclases (ACs) generate cAMP that diffuses throughout the cell. The availability of cAMP activates various intracellular effectors, including protein kinase A (PKA). Specificity in PKA action is achieved by the localization of the enzyme near its substrates through association with A-kinase anchoring proteins (AKAPs). Here, we provide evidence for interactions between AKAP79/150 and ACV and ACVI. PKA anchoring facilitates the preferential phosphorylation of AC to inhibit cAMP synthesis. Real-time cellular imaging experiments show that PKA anchoring with the cAMP synthesis machinery ensures rapid termination of cAMP signaling upon activation of the kinase. This protein configuration permits the formation of a negative feedback loop that temporally regulates cAMP production.
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