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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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mAKAP assembles a protein kinase A/PDE4 phosphodiesterase cAMP signaling module.

Spatiotemporal regulation of protein kinase A (PKA) activity involves the manipulation of compartmentalized cAMP pools. Now we demonstrate that the muscle-selective A-kinase anchoring protein, mAKAP, maintains a cAMP signaling module, including PKA and the rolipram-inhibited cAMP-specific phosphodiesterase (PDE4D3) in heart tissues. Functional analyses indicate that tonic PDE4D3 activity reduces the activity of the anchored PKA holoenzyme, whereas kinase activation stimulates mAKAP-associated phosphodiesterase activity. Disruption of PKA- mAKAP interaction prevents this enhancement of PDE4D3 activity, suggesting that the proximity of both enzymes in the mAKAP signaling complex forms a negative feedback loop to restore basal cAMP levels.[1]

References

  1. mAKAP assembles a protein kinase A/PDE4 phosphodiesterase cAMP signaling module. Dodge, K.L., Khouangsathiene, S., Kapiloff, M.S., Mouton, R., Hill, E.V., Houslay, M.D., Langeberg, L.K., Scott, J.D. EMBO J. (2001) [Pubmed]
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