cAMP-stimulated protein phosphatase 2A activity associated with muscle A kinase-anchoring protein (mAKAP) signaling complexes inhibits the phosphorylation and activity of the cAMP-specific phosphodiesterase PDE4D3.

@article{DodgeKafka2010cAMPstimulatedPP,
  title={cAMP-stimulated protein phosphatase 2A activity associated with muscle A kinase-anchoring protein (mAKAP) signaling complexes inhibits the phosphorylation and activity of the cAMP-specific phosphodiesterase PDE4D3.},
  author={Kimberly L Dodge-Kafka and Andrea L. Bauman and Nicole C Mayer and E. Curtis Henson and Lorena A Heredia and Jung Ja Ahn and Thomas McAvoy and Angus C. Nairn and Michael S Kapiloff},
  journal={The Journal of biological chemistry},
  year={2010},
  volume={285 15},
  pages={
          11078-86
        }
}
The concentration of the second messenger cAMP is tightly controlled in cells by the activity of phosphodiesterases. We have previously described how the protein kinase A-anchoring protein mAKAP serves as a scaffold for the cAMP-dependent protein kinase PKA and the cAMP-specific phosphodiesterase PDE4D3 in cardiac myocytes. PKA and PDE4D3 constitute a negative feedback loop whereby PKA-catalyzed phosphorylation and activation of PDE4D3 attenuate local cAMP levels. We now show that protein… CONTINUE READING
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