The mammalian focal adhesion kinase (FAK) family of nonreceptor protein-tyr
osine kinases have been implicated in controlling a multitude of cellular r
esponses to the engagement of cell surface integrins and G protein-coupled
receptors. We describe here a Drosophila melanogaster FAK homologue, DFak56
, which maps to band 56D on the right arm of the second chromosome. Full-le
ngth DFak56 cDNA encodes a phosphoprotein of 140 kDa, which shares strong s
equence similarity not only with mammalian p125(FAK) but also with the more
recently described mammalian Pyk2 (also known as CAR beta, RAFTK, FAK2, an
d CADTK) FAK family member. DFak56 has intrinsic tyrosine kinase activity a
nd is phosphorylated on tyrosine in vivo. As is the case for FAK, tyrosine
phosphorylation of DFak56 is increased upon plating Drosophila embryo cells
on extracellular matrix proteins. In situ hybridization and immunofluoresc
ence staining analysis showed that DFak56 is ubiquitously expressed with pa
rticularly high levels within the developing central nervous system, We uti
lized the UAS-GAIA expression system to express DFak56 and analyze its func
tion in vivo. Overexpression of DFak56 in the wing imaginal disc results in
wing blistering in adults, a phenotype also observed with both position-sp
ecific integrin loss of function and position-specific integrin overexpress
ion. Our results imply a role for DFak56 in adhesion-dependent signaling pa
thways in viva during D. melanogaster development.