An essential heparin-binding domain in the fibroblast growth factor receptor kinase. Academic Article uri icon

abstract

  • Heparin or heparin-like heparan sulfate proteoglycans are obligatory for activity of the heparin-binding fibroblast growth factor (FGF) family. Heparin interacts independently of FGF ligand with a specific sequence (K18K) in one of the immunoglobulin-like loops in the extracellular domain of the FGF receptor tyrosine kinase transmembrane glycoprotein. A synthetic peptide corresponding to K18K inhibited heparin and heparin-dependent FGF binding to the receptor. K18K and an antibody to K18K were antagonists of FGF-stimulated cell growth. Point mutations of lysine residues in the K18K sequence abrogated both heparin- and ligand-binding activities of the receptor kinase. The results indicate that the FGF receptor is a ternary complex of heparan sulfate proteoglycan, tyrosine kinase transmembrane glycoprotein, and ligand.

published proceedings

  • Science

altmetric score

  • 3

author list (cited authors)

  • Kan, M., Wang, F., Xu, J., Crabb, J. W., Hou, J., & McKeehan, W. L.

citation count

  • 480

complete list of authors

  • Kan, M||Wang, F||Xu, J||Crabb, JW||Hou, J||McKeehan, WL

publication date

  • March 1993