Human Fibroblast Growth Factor Receptor 4 (FGFR4) Protein

Background

Fibroblast growth factor receptor 4 (FGFR4) FGFR4 is a member of the fibroblast growth factor receptor (FGFR) family, characterized as a transmembrane tyrosine kinase receptor that binds FGFs to regulate cell proliferation, differentiation, migration, and survival. Structurally, FGFR4 consists of an extracellular ligand-binding domain composed of three immunoglobulin-like loops, a single transmembrane domain, and an intracellular tyrosine kinase domain. FGFR4 plays essential roles in embryonic development, metabolism, and tissue homeostasis, particularly in liver, muscle, and endocrine tissues. Ligand binding activates downstream signaling cascades, including the MAPK, PI3K-AKT, and STAT pathways, which are critical for cell growth and survival. Dysregulation of FGFR4 signaling has been implicated in various cancers, such as hepatocellular carcinoma and rhabdomyosarcoma, where overexpression or mutation drives tumor growth and metastasis. Its selective expression in specific tissues and its involvement in metabolic regulation, including bile acid synthesis, highlight its specialized biological functions and potential as a therapeutic target in oncology and metabolic disorders.