The tubulogenic activity associated with an activated form of Flt-1 kinase is dependent on focal adhesion kinase.

Focal adhesion kinase (FAK) is known to be located at the intersection between extracellular matrix and growth factor signaling pathways to regulate cell motility. We have shown previously that an activated form (BCR-FLTm1) of Flt-1 kinase, a receptor for vascular endothelial growth factor, had a tubulogenic activity not only in endothelial cells but also in fibroblastic cells. Here we show that tubulogenesis by BCR-FLTm1 depends on FAK and that FAK tyrosine phosphorylation and association with an activated Flt-1 receptor complex is increased after vascular endothelial growth factor stimulation of NIH3T3 cells overexpressing Flt-1.