PIKE mediates EGFR proliferative signaling in squamous cell carcinoma cells

Oncogene. 2012 Dec 6;31(49):5090-8. doi: 10.1038/onc.2012.10. Epub 2012 Feb 20.

Abstract

One of the key drivers for squamous cell carcinoma (SCC) proliferation is activation of the epidermal growth factor receptor (EGFR), a known proto-oncogene. However, the mechanism of EGFR-dependent SCC proliferation remains unclear. Our previous studies indicate that epidermal growth factor (EGF)-induced SCC cell proliferation requires the SH3 domain of phospholipase C-γ1 (PLC-γ1), but not its catalytic activity. The SH3 domain of PLC-γ1 is known to activate the short form of nuclear phosphatidylinositol 3-kinase enhancer (PIKE) that enhances the activity of nuclear class Ia phosphatidylinositol 3-kinase (PI3K) required for proliferation. However, PIKE has been described for more than a decade to be present exclusively in neuronal cells. In the present study, we found that PIKE was highly expressed in malignant human keratinocytes (SCC4 and SCC12B2) but had low expression in normal human keratinocytes. Immunohistochemical analysis showed strong nuclear staining of PIKE in human epidermal and tongue SCC specimens but little staining in the adjacent non-cancerous epithelium. Treatment of SCC4 cells with EGF-induced translocation of PLC-γ1 to the nucleus and binding of PLC-γ1 to the nuclear PIKE. Knockdown of PLC-γ1 or PIKE blocked EGF-induced activation of class Ia PI3K and protein kinase C-ζ and phosphorylation of nucleolin in the nucleus as well as EGF-induced SCC cell proliferation. However, inhibition of the catalytic activity of PLC-γ1 had little effect. These data suggest that PIKE has a critical role in EGF-induced SCC cell proliferation and may function as a proto-oncogene in SCC.

Publication types

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

MeSH terms

  • Carcinoma, Squamous Cell / drug therapy
  • Carcinoma, Squamous Cell / metabolism*
  • Carcinoma, Squamous Cell / pathology*
  • Cell Nucleus / metabolism
  • Cell Proliferation
  • Epidermal Growth Factor / pharmacology
  • Epithelial Cells / drug effects
  • Epithelial Cells / metabolism
  • ErbB Receptors / metabolism*
  • GTP-Binding Proteins / genetics
  • GTP-Binding Proteins / metabolism*
  • GTPase-Activating Proteins / genetics
  • GTPase-Activating Proteins / metabolism*
  • Gene Knockdown Techniques
  • Humans
  • Keratinocytes / drug effects
  • Keratinocytes / metabolism
  • Keratinocytes / pathology
  • Nucleolin
  • Phosphatidylinositol 3-Kinase / metabolism
  • Phospholipase C gamma / genetics
  • Phospholipase C gamma / metabolism
  • Phosphoproteins / metabolism
  • Phosphorylation
  • Protein Kinase C / metabolism
  • Proto-Oncogene Mas
  • RNA-Binding Proteins / metabolism
  • Reference Values
  • Signal Transduction
  • Tongue Neoplasms / metabolism
  • Tongue Neoplasms / pathology
  • src Homology Domains

Substances

  • GTPase-Activating Proteins
  • MAS1 protein, human
  • Phosphoproteins
  • Proto-Oncogene Mas
  • RNA-Binding Proteins
  • Epidermal Growth Factor
  • Phosphatidylinositol 3-Kinase
  • EGFR protein, human
  • ErbB Receptors
  • protein kinase C zeta
  • Protein Kinase C
  • Phospholipase C gamma
  • AGAP2 protein, human
  • GTP-Binding Proteins