Fibroblast growth factor receptor 1 (FGFR1), Fibroblast growth factor receptor 2 (FGFR2), Fibroblast growth factor receptor 3 (FGFR3), Fibroblast growth factor receptor 4 (FGFR4) (FGFR1, FGFR2, FGFR3, FGFR4)

Fibroblast growth factor receptors 1, 2, 3, and 4 are members of the receptor tyrosine kinase superfamily and mediate cell signaling in response to 18 known fibroblast growth factors. Each receptor consists of an extracellular ligand-binding region composed of three immunoglobulin-like domains, a single transmembrane helix, and an intracellular split tyrosine kinase domain. Upon ligand binding, FGFRs dimerize and trans-autophosphorylate, activating multiple downstream signaling pathways (including PLCγ, PI3K–AKT, RAS–MAPK), regulating cellular proliferation, differentiation, migration, and survival. These receptors are critical for development and tissue homeostasis, and their dysregulation is implicated in cancer, developmental syndromes, and other diseases. FGFR1–4 are established drug targets in oncology, with several selective inhibitors approved or in clinical trials. Abnormal FGFR signaling, due to mutations, amplifications, or fusions, drives tumorigenesis and alters tissue growth. Some safety concerns include excessive phosphate retention and ocular effects, reflecting the physiological roles of FGFRs in normal tissues[1][2][3][4][5][6][8].

Other names

FGFR-1, FGFR-2, FGFR-3, FGFR-4CD331, CD332, CD333, CD334CEK1, CEK2HBGFRhydroxyaryl-protein kinaseJTK4 (for FGFR3 specifically)

Inhibition of FGFR tyrosine kinase activity (prevents phosphorylation and downstream signaling); Blockade of FGF binding and receptor dimerization; Induction of cell cycle arrest and apoptosis in tumor cells with FGFR alterations