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

Betty B. Alajajian, Lauren Fletcher, Elif Isgor, David F. Jimenez, Murat Digicaylioglu

Research output: Contribution to journalArticlepeer-review

3 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)579-583
Number of pages5
Issue number6
StatePublished - Apr 22 2009
Externally publishedYes


  • 3'-Phosphoinositide-dependent protein kinase-1
  • AGC kinase
  • AKT
  • Apoptosis
  • Insulin-like growth factor-I
  • Neuroprotection
  • Phosphorylation
  • Protein kinase B
  • Signal transduction

ASJC Scopus subject areas

  • Neuroscience(all)


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