Focal adhesion kinase (FAK) is a non-receptor protein-tyrosine kinase implicated in signaling pathways involved in cell motility, proliferation and apoptosis (1). FAK is composed of a central catalytic domain flanked by large N- and C-terminal regions. FAK is activated by phosphorylation at tyrosine 397 in response to integrin clustering which can be induced by cell adhesion or antibody cross-linking or via G-protein-coupled receptor (GPCR) occupancy by ligands such as bombesin or lysophosphatidic acid (2-3). Phosphorylation of FAK Tyr-397 creates a binding site for Src-family kinases, and phosphorylation of FAK Tyr-576/Tyr-577 in the kinase domain activation loop enhances catalytic activity (4). Increased FAK expression has been correlated with the enhanced motility and invasiveness of human tumor cells, as well as with promoting increased cell proliferation.
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Western blot analysis on human brain tissue lysates (A, B) and rat brain tissue lysates (C, D) using anti-Phospho-Fak (pY397), 1:2000 dilution. Cells were either (A, C) untreated (B, D) treated with AP
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