Fibroblast Growth Factor Receptors (FGFRs) are a group of transmembrane receptor proteins that play a crucial role in various cellular processes, particularly in cell growth, development, and regeneration. These receptors belong to the family of receptor tyrosine kinases (RTKs) and are activated by a family of proteins called fibroblast growth factors (FGFs).
FGFRs are composed of an extracellular domain, a transmembrane domain, and an intracellular domain. The extracellular domain consists of three immunoglobulin-like domains (D1-D3), which are responsible for binding with FGF ligands. The intracellular domain possesses a kinase domain, which upon activation by ligand binding, initiates a signaling cascade leading to various cellular responses.
There are four known types of FGFRs, namely FGFR1, FGFR2, FGFR3, and FGFR4, each with different tissue distribution and ligand specificity. These receptors are widely expressed in various tissues and organs, including the brain, heart, skeletal system, and reproductive system. They are involved in the regulation of cell proliferation, differentiation, survival, and migration.
Aberrant FGFR signaling has been implicated in a range of diseases, including cancer, skeletal disorders, developmental abnormalities, and certain genetic syndromes. Consequently, FGFRs have become attractive targets for therapeutic intervention. Inhibitors that specifically target FGFRs are being developed as potential treatments for cancers with FGFR gene alterations or overexpression, making them an important focus of research in the field of oncology.
