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Fibroblast growth factors (FGFs) are a family of structurally related polypeptide growth factors with diverse roles in regulating cell proliferation, migration, differentiation, and apoptosis. FGFs exert their functions by binding to FGF receptors (FGFRs) with heparin/heparan sulfate as a cofactor. Upon activation, FGFRs recruit specific molecules to phosphorylated tyrosine residues in the cytosolic domain, triggering multiple signaling pathways—including RAS-MAPK, PI3K-AKT, PLCγ, and STAT—and leading to specific cellular responses. The mammalian Fgf family comprises 22 genes, 18 of which encode proteins (FGF1–FGF10 and FGF16–FGF23) that signal through four highly conserved transmembrane tyrosine kinase receptors (FGFR1, FGFR2, FGFR3, and FGFR4). The FGF homologous factors (FGF11, FGF12, FGF13, and FGF14) share high sequence identity with the FGF family but do not activate FGFRs and are therefore not generally considered members of the FGF family. FGFs are highly conserved in both gene structure and amino acid sequence across vertebrate species.