What is Human Fibroblast Growth Factor Receptor and its biological function

Human Fibroblast Growth Factor Receptor is a transmembrane protein that is involved in the regulation of cell growth and development. It is part of the fibroblast growth factor (FGF) family of receptors and is important in cell signaling pathways. When a ligand, such as FGF, binds to the receptor, it triggers a signaling cascade that leads to the activation of several downstream pathways, including the MAPK, PI3K/Akt, and JAK/STAT pathways. These pathways are involved in cell growth, proliferation, differentiation, and survival.

FGFR1 is a single-pass transmembrane glycoprotein composed of an extracellular ligand-binding domain, a transmembrane domain and an intracellular tyrosine kinase domain. The extracellular domain consists of three immunoglobulin-like domains and two fibronectin type III domains, while the transmembrane domain consists of a single alpha-helix. The intracellular domain contains a tyrosine kinase domain, which is responsible for the receptor's enzymatic activity.

Recent research into FGFR1 has focused on its role in the regulation of cell growth and development, and its potential to treat a variety of diseases. Studies have shown that FGFR1 mutations can cause a variety of diseases, such as achondroplasia, craniosynostosis, and Muenke syndrome. Additionally, FGFR1 has been linked to the development of certain types of cancers, such as bladder cancer, non-small cell lung cancer, and head and neck squamous cell carcinoma.

Currently, several drugs have been approved by the US Food and Drug Administration (FDA) for targeting FGFR1. These include erdafitinib, which is used to treat metastatic bladder cancer, and lenvatinib and cabozantinib, which are used in combination with other treatments to treat advanced renal cell carcinoma. Additionally, pemigatinib is used to treat metastatic cholangiocarcinoma, and vemurafenib is used to treat metastatic melanoma.