Abstract
mAKAP (muscle-selective A-kinase-anchoring protein) co-ordinates a cAMP-sensitive negative-feedback loop comprising PKA (cAMP-dependent protein kinase) and the cAMP-selective PDE4D3 (phosphodiesterase 4D3). In vitro and cellular experiments demonstrate that PKA-phosphorylation of PDE4D3 on Ser-13 increases the affinity of PDE4D3 for mAKAP. Our data suggest that activation of mAKAP-anchored PKA enhances the recruitment of PDE4D3, allowing for quicker signal termination.
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Carlisle Michel, J. J., Dodge, K. L., Wong, W., Mayer, N. C., Langeberg, L. K., & Scott, J. D. (2004). PKA-phosphorylation of PDE4D3 facilitates recruitment of the mAKAP signalling complex. Biochemical Journal, 381(3), 587–592. https://doi.org/10.1042/BJ20040846
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