FGFR-4 Protein, Mouse (HEK293, His)

FGFR-4 Protein is a tyrosine-protein kinase that acts as a cell-surface receptor for fibroblast growth factors, regulating cell proliferation, differentiation, migration, lipid metabolism, bile acid biosynthesis, glucose uptake, vitamin D metabolism, and phosphate homeostasis. It is essential for the normal down-regulation of CYP7A1 expression, the enzyme involved in bile acid synthesis, in response to FGF19. Upon ligand binding, FGFR-4 phosphorylates PLCG1 and FRS2, leading to the activation of multiple signaling cascades. Activation of PLCG1 results in the production of diacylglycerol and inositol 1,4,5-trisphosphate. Phosphorylation of FRS2 recruits GRB2, GAB1, PIK3R1, and SOS1, activating the RAS, MAPK1/ERK2, MAPK3/ERK1, and AKT1 signaling pathways. FGFR-4 also facilitates the SRC-dependent phosphorylation and lysosomal degradation of MMP14, a matrix protease, with MMP14 aiding in the internalization and degradation of FGFR-4. In addition, FGFR-4 plays a role in postnatal lung development and may be involved in skeletal muscle cell lineage development.