FGFR2 encodes a receptor tyrosine kinase with tissue-specific isoform switching that determines ligand specificity.
| Isoform | UniProt ID | Exon Usage | Ligand Specificity | Tissue Expression |
|---|---|---|---|---|
| FGFR2IIIb | P21802-1 | Exon IIIb | FGF1, FGF3, FGF7 (KGF), FGF10 | EPITHELIAL |
| FGFR2IIIc | P21802-3 | Exon IIIc | FGF1, FGF2, FGF4, FGF6, FGF9 | MESENCHYMAL |
The Ig-like domain III is alternatively spliced:
- Exon IIIb encodes epithelial-specific splice variant
- Exon IIIc encodes mesenchymal-specific splice variant
This creates mutually exclusive ligand binding:
- FGF7 (KGF) binds ONLY to IIIb (epithelial)
- FGF2 binds preferentially to IIIc (mesenchymal)
The IIIb/IIIc isoform switching enables paracrine signaling:
- Mesenchyme produces FGF7/10 → signals to epithelium (IIIb)
- Epithelium produces FGF2/4 → signals to mesenchyme (IIIc)
This is critical for:
- Limb development
- Lung branching morphogenesis
- Prostate development
- Wound healing
These may act as decoy receptors, similar to soluble FAS.
Isoform switching in cancer:
- Epithelial-to-mesenchymal transition (EMT) includes IIIb→IIIc switch
- Some cancers inappropriately express IIIc in epithelial contexts
- Mis-splicing correlates with metastatic potential