Inhibition of focal adhesion kinase (FAK) signaling in focal adhesions decreases cell motility and proliferation

Andrew P. Gilmore, Lewis H. Romer

Research output: Contribution to journalArticlepeer-review

452 Scopus citations


It has been proposed that the focal adhesion kinase (FAK) mediates focal adhesion formation through tyrosine phosphorylation during cell adhesion. We investigated the role of FAK in focal adhesion structure and function. Loading cells with a glutathione-S-transferase fusion protein (GST-Cterm) containing the FAK focal adhesion targeting sequence, but not the kinase domain, decreased the association of endogenous FAK with focal adhesions. This displacement of endogenous FAK in both BALB/c 3T3 cells and human umbilical vein endothelial cells loaded with GST-Cterm decreased focal adhesion phosphotyrosine content. Neither cell type, however, exhibited a reduction in focal adhesions after GST-Cterm loading. These results indicate that FAK mediates adhesion-associated tyrosine phosphorylation, but not the formation of focal adhesions. We then examined the effect of inhibiting FAK function on other adhesion-dependent cell behavior. Cells microinjected with GST-Cterm exhibited decreased migration. In addition, cells injected with GST-Cterm had decreased DNA synthesis compared with control-injected or noninjected cells. These findings suggest that FAK functions in the regulation of cell migration and cell proliferation.

Original languageEnglish (US)
Pages (from-to)1209-1224
Number of pages16
JournalMolecular biology of the cell
Issue number8
StatePublished - Aug 1996
Externally publishedYes

ASJC Scopus subject areas

  • General Medicine


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