Non-receptor protein-tyrosine kinase implicated in signaling pathways involved in cell motility, proliferation and apoptosis. 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. Microtubule-induced dephosphorylation at Tyr-397 is crucial for the induction of focal adhesion disassembly. Plays a potential role in oncogenic transformations resulting in increased kinase activity.
Expressed in all organs tested, in lymphoid cell lines, but most abundantly in brain.
Belongs to the protein kinase superfamily. Tyr protein kinase family. FAK subfamily. Contains 1 FERM domain. Contains 1 protein kinase domain.
The first Pro-rich domain interacts with the SH3 domain of CRK-associated substrate (BCAR1) and CASL. The carboxy-terminal region is the site of focal adhesion targeting (FAT) sequence which mediates the localization of FAK1 to focal adhesions.
Phosphorylated on 6 tyrosine residues upon activation. Microtubule-induced dephosphorylation at Tyr-397 could be catalyzed by PTPN11 and regulated by ZFYVE21. Dephosphorylated by PTPN11 upon EPHA2 activation by its ligand EFNA1.
Wu J et al. AURKA promotes cell migration and invasion of head and neck squamous cell carcinoma through regulation of the AURKA/Akt/FAK signaling pathway. Oncol Lett11:1889-1894 (2016).
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