Tyrosine-protein kinase FGFR4 functions as a cell-surface receptor for fibroblast growth factors (FGFs), regulating cell proliferation, differentiation, migration, and key metabolic processes such as lipid metabolism, bile acid biosynthesis, glucose uptake, vitamin D metabolism, and phosphate homeostasis. It is essential for suppressing CYP7A1 expression, the rate-limiting enzyme in bile acid synthesis, in response to FGF19.
FGFR4 phosphorylates PLCG1 and FRS2 upon ligand binding, activating multiple signaling pathways. PLCG1 activation produces diacylglycerol and inositol 1,4,5-trisphosphate, while FRS2 phosphorylation recruits GRB2, GAB1, PIK3R1, and SOS1, driving RAS, MAPK/ERK, and AKT1 signaling. FGFR4 also promotes SRC-dependent phosphorylation and lysosomal degradation of MMP14, which in turn facilitates FGFR4 internalization and degradation to regulate signaling.
Mutations causing constitutive kinase activation or impaired inactivation lead to aberrant signaling, contributing to pathological processes. FGFR4’s regulated activity underscores its critical role in cellular and metabolic homeostasis.
| Product Name | Recombinant Human FGFR4 Protein |
| Accession | P22455 |
| Host Species | Human |
| Gene | FGFR4 |
| Source | Sf9 |
