Protein kinase C theta (PKCtheta)-dependent phosphorylation of PDK1 at Ser504 and Ser532 contributes to palmitate-induced insulin resistance.

@article{Wang2009ProteinKC,
  title={Protein kinase C theta (PKCtheta)-dependent phosphorylation of PDK1 at Ser504 and Ser532 contributes to palmitate-induced insulin resistance.},
  author={Changhua Wang and Meilian Liu and Ramon A. Riojas and Xiaoban Xin and Zhanguo Gao and Rong Zeng and Jiarui Wu and Lily Q. Dong and Feng Liu},
  journal={The Journal of biological chemistry},
  year={2009},
  volume={284 4},
  pages={2038-44}
}
Clinical, epidemiological, and biochemical studies have highlighted the role of obesity-induced insulin resistance in various metabolic diseases. However, the underlying molecular mechanisms remain to be established. In the present study, we show that palmitate-induced serine phosphorylation of phosphoinositide-dependent protein kinase-1 (PDK1) negatively regulates insulin signaling. PDK1-mediated Akt phosphorylation at Thr308 in the activation loop is reduced in C2C12 myotubes treated with… CONTINUE READING