Disruption of protein kinase A interaction with A-kinase-anchoring proteins in the heart in vivo: effects on cardiac contractility, protein kinase A phosphorylation, and troponin I proteolysis.

@article{McConnell2009DisruptionOP,
  title={Disruption of protein kinase A interaction with A-kinase-anchoring proteins in the heart in vivo: effects on cardiac contractility, protein kinase A phosphorylation, and troponin I proteolysis.},
  author={Bradley K. McConnell and Zoran Popovi{\'c} and Niladri Mal and Kwangdeok Lee and James A. Bautista and Farhad Forudi and Ra{\'u}l Schwartzman and Jian-Ping Jin and Marc Penn and Meredith Bond},
  journal={The Journal of biological chemistry},
  year={2009},
  volume={284 3},
  pages={1583-92}
}
Protein kinase A (PKA)-dependent phosphorylation is regulated by targeting of PKA to its substrate as a result of binding of regulatory subunit, R, to A-kinase-anchoring proteins (AKAPs). We investigated the effects of disrupting PKA targeting to AKAPs in the heart by expressing the 24-amino acid regulatory subunit RII-binding peptide, Ht31, its inactive analog, Ht31P, or enhanced green fluorescent protein by adenoviral gene transfer into rat hearts in vivo. Ht31 expression resulted in loss of… CONTINUE READING
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