FGFR-4 Protein, Rat (HEK293, hFc)

FGFR-4 protein, a tyrosine-protein kinase, functions as a cell-surface receptor for fibroblast growth factors, playing a crucial role in the regulation of cell proliferation, differentiation, and migration. Additionally, it contributes to the control of lipid metabolism, bile acid biosynthesis, glucose uptake, vitamin D metabolism, and phosphate homeostasis. Its significance is highlighted in the normal down-regulation of CYP7A1, the rate-limiting enzyme in bile acid synthesis, in response to FGF19. Upon ligand binding, FGFR-4 activates various signaling cascades, including the phosphorylation of PLCG1 and FRS2. This activation leads to the production of cellular signaling molecules like diacylglycerol and inositol 1,4,5-trisphosphate. Furthermore, FRS2 phosphorylation triggers the recruitment of GRB2, GAB1, PIK3R1, and SOS1, activating RAS, MAPK1/ERK2, MAPK3/ERK1, the MAP kinase signaling pathway, and the AKT1 signaling pathway. Notably, FGFR-4 promotes SRC-dependent phosphorylation of the matrix protease MMP14, facilitating its lysosomal degradation. To regulate FGFR-4 signaling, the receptor undergoes internalization and degradation, a process facilitated by MMP14.