Exon skipping causes alteration of the COOH-terminus and deletion of the phospholipase C gamma 1 interaction site in the FGF receptor 2 kinase in normal prostate epithelial cells.

Polymerase chain reaction analysis revealed an mRNA in rat prostate that results from alternate splicing of exon 16 in the heparin-binding fibroblast growth factor receptor kinase type 2 gene (FGFR2). The absence of exon 16 and the shift in reading frame at the exon 15-17 junction predicts an expression product (FGFR2-2) with a unique COOH-terminus that does not exhibit the major autophosphorylation site (tyrosine 789) required for interaction of phospholipase C gamma 1 with the full-length FGFR2-1 isoform. Nuclease protection analysis revealed that the FGFR-2 splice variant is expressed in quantities equal to or greater than the FGFR2-1 isoform in normal prostate tissue. When combined with the same FGFR2 extracellular domain, co-expression of the two COOH-terminal variants may mediate effect of the same FGF ligand on different signal transduction pathways.