Human Fibroblast Growth Factor Receptor 1 (FGFR1) Enzyme

Background

Fibroblast growth factor receptor 1 (FGFR1) FGFR1 is a transmembrane tyrosine kinase receptor that binds fibroblast growth factors (FGFs), playing a critical role in cellular proliferation, differentiation, and survival. FGFR1 consists of an extracellular ligand-binding domain composed of three immunoglobulin-like loops, a single transmembrane helix, and an intracellular tyrosine kinase domain. Upon FGF binding, FGFR1 undergoes dimerization and autophosphorylation, triggering downstream signaling pathways such as the MAPK, PI3K-AKT, and PLCγ pathways. FGFR1 is essential in embryonic development, angiogenesis, and tissue repair, and its dysregulation is implicated in various cancers, including lung and breast cancer, where aberrant FGFR1 activation promotes tumor growth and survival. FGFR1 is also involved in skeletal development, and mutations in the FGFR1 gene can lead to developmental disorders such as Pfeiffer syndrome. Its widespread expression in multiple tissues highlights its diverse biological roles.