Phosphorylation of the protein kinase C-theta activation loop and hydrophobic motif regulates its kinase activity, but only activation loop phosphorylation is critical to in vivo nuclear-factor-kappaB induction.

@article{Liu2002PhosphorylationOT,
  title={Phosphorylation of the protein kinase C-theta activation loop and hydrophobic motif regulates its kinase activity, but only activation loop phosphorylation is critical to in vivo nuclear-factor-kappaB induction.},
  author={Yin Liu and Caroline Graham and Aiqun Li and Robert J. Fisher and S. J. Shaw},
  journal={The Biochemical journal},
  year={2002},
  volume={361 Pt 2},
  pages={255-65}
}
Protein kinase C (PKC)-theta, a member of the 'novel' subfamily of PKC isoforms, is of singular importance in transducing signals in T-lymphocytes. Since understanding of regulatory phosphorylation of novel PKCs is fragmentary and inconsistent with findings for 'classical' PKC isoforms, we investigated three potential phosphorylation sites on PKC-theta; in… CONTINUE READING