Cross-regulation of novel protein kinase C (PKC) isoform function in cardiomyocytes. Role of PKC epsilon in activation loop phosphorylations and PKC delta in hydrophobic motif phosphorylations.

@article{Rybin2003CrossregulationON,
  title={Cross-regulation of novel protein kinase C (PKC) isoform function in cardiomyocytes. Role of PKC epsilon in activation loop phosphorylations and PKC delta in hydrophobic motif phosphorylations.},
  author={Vitalyi O. Rybin and Abdelkarim Sabri and Jacob Short and Julian C. Braz and Jeffery D Molkentin and Susan F. Steinberg},
  journal={The Journal of biological chemistry},
  year={2003},
  volume={278 16},
  pages={14555-64}
}
Recent studies identify conventional protein kinase C (PKC) isoform phosphorylations at conserved residues in the activation loop and C terminus as maturational events that influence enzyme activity and targeting but are not dynamically regulated by second messengers. In contrast, this study identifies phorbol 12-myristoyl 13-acetate (PMA)- and norepinephrine-induced phosphorylations of PKC epsilon (at the C-terminal hydrophobic motif) and PKC delta (at the activation loop) as events that… CONTINUE READING
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