Antagonistic effect of EGF on FAK phosphorylation/dephosphorylation in a cell

Sang Heon Kim, Soo Hyun Kim

Research output: Contribution to journalArticlepeer-review

19 Citations (Scopus)


Focal adhesion kinase (FAK) plays a key role in the crosstalk of growth factor- and cell adhesion-mediated signaling pathway. In this study, we found that the quantitative change of phosphorylated FAK was bell-shaped time-dependently by EGF stimulation in immortalized human keratinocyte (HaCaT). EGF enhanced FAK phosphorylation and cell spreading in adhering HaCaT cells with low-phosphorylated FAK. On the other hand, spread HaCaT cells having high-phosphorylated FAK changed to round shapes with FAK dephosphorylation 15 min after EGF stimulation. Pharmacological agents, U0126 and PD98059 (mitogen-activated protein kinases (MAPK) kinases (MEK) inhibitors), and AG1478 (an EGF receptor kinase inhibitor) blocked the cell rounding and FAK dephosphorylation. In addition, the EGFR-MAPK signaling pathway had an influence on cell migration by regulating FAK dephosphorylation of keratinocytes in response of EGF, since the MEK inhibitors and AG1478 suppressed EGF-induced cell migration. However, FAK phosphorylation and HaCaT cell spreading were inhibited only by the antagonist of EGF - EGFR binding but not by the MEK inhibitors and AG1478. Taken together, we suggest that EGF is antagonistically involved in both FAK phosphorylation and dephosphorylation with different mechanisms in a cell.

Original languageEnglish
Pages (from-to)539-547
Number of pages9
JournalCell Biochemistry and Function
Issue number5
Publication statusPublished - 2008 Jul
Externally publishedYes


  • Cell adhesion
  • Cell migration
  • Dephosphorylation
  • EGF receptor
  • Epidermal growth factor
  • Focal adhesion kinase
  • Phosphorylation

ASJC Scopus subject areas

  • Biochemistry
  • Clinical Biochemistry
  • Cell Biology


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