Phosphorylation of protein kinase N by phosphoinositide-dependent protein kinase-1 mediates insulin signals to the actin cytoskeleton.

@article{Dong2000PhosphorylationOP,
  title={Phosphorylation of protein kinase N by phosphoinositide-dependent protein kinase-1 mediates insulin signals to the actin cytoskeleton.},
  author={L. Dong and L. R. Landa and M. Wick and L. Zhu and H. Mukai and Y. Ono and F. Liu},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2000},
  volume={97 10},
  pages={
          5089-94
        }
}
  • L. Dong, L. R. Landa, +4 authors F. Liu
  • Published 2000
  • Biology, Medicine
  • Proceedings of the National Academy of Sciences of the United States of America
Growth factors such as insulin regulate phosphatidylinositol 3-kinase-dependent actin cytoskeleton rearrangement in many types of cells. However, the mechanism by which the insulin signal is transmitted to the actin cytoskeleton remains largely unknown. Yeast two-hybrid screening revealed that the phosphatidylinositol 3-kinase downstream effector phosphoinositide-dependent protein kinase-1 (PDK1) interacted with protein kinase N (PKN), a Rho-binding Ser/Thr protein kinase potentially implicated… Expand
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