Focal adhesion kinase (pp125(FAK) Or FAK) is a protein tyrosine kinase whic
h is associated with intracellular signalling cascades which are initiated
when the integrin family of cell adhesion molecules engage extracellular ma
trix molecules. In cultured cells, this molecule is physically associated w
ith focal adhesions, which are well-defined regions of intimate cell-to-sub
stratum adhesion. In this location, it interacts with other proteins of the
focal adhesion to activate intracellular signalling events associated with
cell adhesion. The in vitro expression of FAK and its level of phosphoryla
tion appear to be related to several physiological phenomena, including cel
l spreading, cell differentiation, cell locomotion and cell death. Because
these phenomena are all of critical importance during morphogenesis, and be
cause FAK is expressed in embryonic cells, evidence has been accumulating t
o indicate that FAK may be an important modulator of developmental processe
s. In this review, this evidence is surveyed together with evidence from an
alogous situations, such as tumour cell migration and invasiveness. Althoug
h evidence suggesting a role for FAK in morphogenesis is accumulating, curr
ent uncertainties regarding its cytoplasmic location and its molecular inte
ractions in vivo make it difficult to reach definitive conclusions regardin
g the significance of its contributions to developmental processes.