IGF-I regulated phosphorylation and translocation of PDK-1 in neurons

Neuroreport. 2009 Apr 22;20(6):579-83. doi: 10.1097/WNR.0b013e328329a41a.

Abstract

3'-phosphoinositide-dependent protein kinase-1 (PDK-1) is a crucial serine/threonine kinase in the insulin-like growth factor-I (IGF-I)/AKT signaling pathway, but its function and localization in the nervous system has not been fully characterized. In this study, we compared the localization of PDK-1 in adult neurons and non-neuronal PC-3 cells. We showed that PC-3 cells expressed phosphorylated and nonphosphorylated PDK-1 in the cytoplasm and nucleoplasm. In contrast, neuronal PDK-1 was located in the nucleoplasm and the phosphorylated form was located along the perinuclear region. Furthermore, we found that IGF-I transiently increased phosphorylation of neuronal PDK-1, resulting in its translocation to other cellular compartments. Our findings suggest that IGF-I may regulate neuronal PDK-1 differently than in non-neuronal cells, which may indicate a novel role for PDK-1 in IGF-I-mediated neuroprotective signaling.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • 3-Phosphoinositide-Dependent Protein Kinases
  • Animals
  • Blotting, Western
  • Cell Line, Tumor
  • Cell Nucleus / metabolism
  • Cell Proliferation
  • Cells, Cultured
  • Cytoplasm / metabolism
  • Fluorescent Antibody Technique
  • Humans
  • Insulin-Like Growth Factor I / metabolism*
  • Neurons / metabolism*
  • Phosphorylation
  • Protein Serine-Threonine Kinases / metabolism*
  • Proto-Oncogene Proteins c-akt / metabolism
  • Rats
  • Rats, Sprague-Dawley

Substances

  • Insulin-Like Growth Factor I
  • 3-Phosphoinositide-Dependent Protein Kinases
  • PDPK1 protein, human
  • Protein Serine-Threonine Kinases
  • Proto-Oncogene Proteins c-akt