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doi: 10.1242/10.1242/jcs.00373

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Focal adhesion kinase: the first ten years

Department of Microbiology, Box 800734, University of Virginia Health System, Charlottesville, VA 22908, USA

View larger version (17K): [in a new window]   Fig. 1. Organization of the domains of focal adhesion kinase. The N-terminal domain shares similarity with members of the FERM homology domain family of proteins and directs interactions with integrins and growth factor receptors. The central domain is the catalytic domain. The C-terminal domain contains sites for multiple protein-protein interactions. Site I (SI) is an interaction site for the SH3 domain of Cas; site II (SII) is the site of interaction with the SH3 domains of GRAF and ASAP. Y397 is the major site of autophosphorylation and a site of interaction with the SH2 domain of Src. FAT denotes the region required for focal adhesion targeting. The inset illustrates the four helical bundle that makes up the FAT domain. Paxillin interacts within sequences with the FAT domain; these sequences are denoted in yellow in the FAT structure. Additional sites of tyrosine and serine phosphorylation are indicated.

View larger version (28K): [in a new window]   Fig. 2. Proposed interactions among the proteins involved in integrin signaling. As indicated in the text, integrins signal through FAK to signaling pathways that regulate small GTPases of the Rho and Arf families. Signals through FAK to Rac and Pak play a role in modulating cell adhesion and migration, actin polymerization and MAP kinse signaling.