Human Fibroblast Growth Factor Receptor 2 (FGFR2) Enzyme

Background

Fibroblast growth factor receptor 2 (FGFR2) FGFR2 is a transmembrane receptor tyrosine kinase that binds fibroblast growth factors (FGFs) to regulate diverse cellular processes such as proliferation, differentiation, migration, and tissue repair. FGFR2 consists of an extracellular ligand-binding domain with three immunoglobulin-like domains, a single-pass transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding induces receptor dimerization and autophosphorylation, initiating downstream signaling cascades such as the MAPK, PI3K-AKT, and PLCγ pathways. FGFR2 is crucial in embryonic development, particularly in limb and craniofacial formation, as well as in tissue homeostasis. Mutations in FGFR2 are associated with skeletal disorders like Apert syndrome and Crouzon syndrome, which result from gain-of-function mutations leading to aberrant signaling. FGFR2 dysregulation is also implicated in cancer, particularly in breast and gastric cancers, where it promotes tumor growth, survival, and angiogenesis. Its tissue-specific splicing variants further contribute to its functional diversity across different biological contexts.