Fibroblast growth factors (FGFs) produce mitogenic and angiogenic effects in target cells by signaling through the cellular surface tyrosine kinase receptors. There are four members of the FGF receptor family: FGFR-1 (flg), FGFR-2 (bek, KGFR), FGFR-3 and FGFR-4. Each receptor contains an extracellular ligand binding domain, a transmembrane region and a cytoplasmic kinase domain (1). Following ligand binding and dimerization, the receptors are phosphorylated at specific tyrosine residues (2). Seven tyrosine residues in the cytoplasmic tail of FGFR-1 can be phosphorylated: Tyr463, Tyr583, Tyr585, Tyr653, Tyr654, Tyr730 and Tyr766. Tyrosine 653 and 654 are important for catalytic activity of the activated FGFR and are essential for signaling (3). The other phosphorylated tyrosine residues may provide docking sites for downstream signaling components such as Crk and PLCgamma.
Synonyms: FGFR1 phospho Y154, FGFR1 phospho Tyr154, p-FGFR1 phospho Y154, bFGF R, BFGFR, C FGR, CD 331, CD331, CD331 antigen, CEK, FGFBR, FGFR 1, Fibroblast growth factor receptor 1, FLG, FLG protein, FLJ14326, FLT 2, FLT2, Fms like tyrosine kinase 2, Fms related tyrosine kinase 2, Fms related tyrosine kinase 2 Pfefer syndrome, H2, H3, H4, H5, HBGFR, Heparin binding growth factor receptor, Hydroxyaryl protein kinase, KAL 2, KAL2, MFR, N SAM, N sam tyrosine kinase, Protein tyrosine kinase, Tyrosylprotein kinase, Basic fibroblast growth factor receptor 1, FGFR1_HUMAN.