Critical role of novel Thr-219 autophosphorylation for the cellular function of PKCtheta in T lymphocytes.

@article{Thuille2005CriticalRO,
  title={Critical role of novel Thr-219 autophosphorylation for the cellular function of PKCtheta in T lymphocytes.},
  author={Nikolaus Thuille and Isabelle Heit and Friedrich Fresser and Nina Krumb{\"o}ck and Birgit Bauer and Sabine Leuthaeusser and Sascha Dammeier and Caroline Graham and Terry D. Copeland and Steve Shaw and Gottfried Baier},
  journal={The EMBO journal},
  year={2005},
  volume={24 22},
  pages={3869-80}
}
Phosphopeptide mapping identified a major autophosphorylation site, phospho (p)Thr-219, between the tandem C1 domains of the regulatory fragment in protein kinase C (PKC)theta. Confirmation of this identification was derived using (p)Thr-219 antisera that reacted with endogenous PKCtheta in primary CD3+ T cells after stimulation with phorbol ester, anti-CD3 or vanadate. The T219A mutation abrogated the capacity of PKCtheta to mediate NF-kappaB, NF-AT and interleukin-2 promoter transactivation… CONTINUE READING
13 Citations
36 References
Similar Papers

Citations

Publications citing this paper.
Showing 1-10 of 13 extracted citations

References

Publications referenced by this paper.
Showing 1-10 of 36 references

Long A (2005) Stimulus-induced phosphorylation of PKCy at the Ser-695 hydrophobic-motif

  • M Freeley, Y Volkov, D Kelleher
  • 2005
1 Excerpt

Stimulus - induced phosphorylation of PKC y at the Ser - 695 hydrophobic - motif in human T lymphocytes

  • K Fujii, G Zhu, +4 authors S Shaw
  • Biochem Biophys Res Commun
  • 2005

PKC y signals activation versus tolerance in vivo

  • K Bi, Y Tanaka, +4 authors A Altman
  • J Exp Med
  • 2004

Phosphorylation of the PKC y activation loop and hydrophobic motif regulates its kinase activity , but only activation loop phosphorylation is critical to in vivo NFk B induction

  • BJ Marsland, TJ Soos, G Spath, DR Littman, M Kopf
  • Biochem J
  • 2004
1 Excerpt

Similar Papers

Loading similar papers…