An essential heparin-binding domain in the fibroblast growth factor receptor kinase

Mikio Kan, Fen Wang, Jianming Xu, John W. Crabb, Jinzhao Hou, Wallace L. McKeehan

Research output: Contribution to journalArticle

463 Scopus citations

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 K1i8K 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.

Original languageEnglish (US)
Pages (from-to)1918-1921
Number of pages4
JournalScience
Volume259
Issue number5103
DOIs
StatePublished - 1993

ASJC Scopus subject areas

  • General

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