FAK: a tyrosine kinase of the FAK family required for cell migration and contact-dependent survival signaling. Activated by tyrosine-phosphorylation in response to either integrin clustering induced by cell adhesion or antibody cross-linking, or via G-protein coupled receptor (GPCR) occupancy by ligands such as bombesin or lysophosphatidic acid, or via LDL receptor occupancy. Downstream of integrins and Src, upstream of Ras/MAPK. Localizes to focal adhesions that form between cells growing in the presence of extracellular matrix constituents. Interacts with CAS family members and with GIT1, SORBS1 and BCAR3. Interacts with Shb. Required for full Ras transformation of fibroblasts. Increased expression in breast and other cancers, related to chromosome 8q amplification. Overexpression and activation associated with increased migration, invasion and progression of ovarian cancer, and with progression in hepatocellular carcinoma, thyroid cancer, and acute myelogenous leukemia. siRNA increases chemosensitivity of pancreatic adenocarcinoma xenografts. Inhibitor: ISI15421 (antisense). Four splice-variant isoforms have been observed.
Protein type: Kinase, protein; Protein kinase, tyrosine (non-receptor); EC 2.7.10.2; Protein kinase, TK; TK group; Fak family
Cellular Component: cell; cytoplasm; extrinsic to internal side of plasma membrane; focal adhesion; microtubule organizing center; nucleus; perinuclear region of cytoplasm; sarcolemma
Molecular Function: ATP binding; calcium-dependent cysteine-type endopeptidase activity; identical protein binding; non-membrane spanning protein tyrosine kinase activity; protease binding; protein binding; protein-tyrosine kinase activity; receptor binding; signal transducer activity
Biological Process: actin filament organization; angiogenesis; angiogenesis involved in wound healing; cell adhesion; cell differentiation; cytoskeleton organization and biogenesis; epidermal growth factor receptor signaling pathway; innate immune response; negative regulation of apoptosis; negative regulation of protein amino acid autophosphorylation; peptidyl-tyrosine phosphorylation; positive regulation of cell proliferation; positive regulation of focal adhesion formation; positive regulation of protein binding; protein amino acid autophosphorylation; proteolysis; pyramidal neuron migration; regulation of cell adhesion; regulation of cell proliferation; response to pH; signal complex assembly
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