Fibroblast growth factor receptor 1 (FGFR1) and Fibroblast growth factor receptor 2 (FGFR2) (FGFR1, FGFR2)

Fibroblast growth factor receptor 1 and fibroblast growth factor receptor 2 are members of the receptor tyrosine kinase (RTK) family that reside on the cell membrane and function as high-affinity receptors for fibroblast growth factors (FGFs)[1][2][3]. Each receptor consists of an extracellular region with three immunoglobulin-like domains that bind FGFs, a single transmembrane helix, and an intracellular tyrosine kinase domain responsible for activating diverse signaling cascades important for embryogenesis, tissue maintenance, and repair[1][2][3]. FGFR1 and FGFR2 signaling regulates processes including cell proliferation, differentiation, and survival, and is crucial for development of muscle, bone, and other tissues[1][3][4]. Pathogenic mutations, gene amplifications, or abnormal activation of FGFR1/2 can cause a range of disorders, notably numerous cancers, skeletal malformations, and developmental defects[1][3]. Drug inhibitors that target their kinase domains are approved or in development for the treatment of various FGFR-driven malignancies, but therapy is challenged by resistance mechanisms and safety concerns[1].

Other names

CD331bFGF receptor 1FLT2CD332KGFR (keratinocyte growth factor receptor)BEK

Tyrosine kinase inhibition: drugs block the kinase activity by binding competitively to the ATP-binding site of FGFR, inhibiting downstream signaling required for tumor or abnormal cell growth[1]. Induction of downstream pathway inhibition (e.g., MAPK, PI3K/AKT)[1][5].