The focal adhesion kinase

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Abstract
The focal adhesion kinase, FAK or pp125FAK, is a 125 kDa protein tyrosine kinase (PTK), whose name is derived from its subcellular localization (Schaller et al. 1992). Although originally identified as a putative substrate for pp60v-src (Kanner et al. 1990), an oncogenic PTK, FAK has gained its notoriety as an element of a signaling pathway regulated by cell surface receptors called integrins (Schaller & Parsons 1993, 1994). Integrins are heterodimeric, transmembrane proteins that can simultaneously bind to proteins of the extracellular matrix (ECM), e.g. fibronectin, and to components of the actin cytoskeleton, e.g. talin and α-actinin (Burridge et al. 1988, Turner & Burridge 1991). In addition to their role in cell adhesion to ECM and in anchoring the cytoskeleton, the integrins can transduce extracellular cues into cytoplasmic signals (Damsky & Werb 1992, Hynes 1992, Schwartz 1992, Juliano & Haskill 1993), which include the tyrosine phosphorylation and enzymatic activation of FAK

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