Signal Transduction by Fibroblast Growth Factor Receptors

Front Biosci. 1999 Feb 15;4:D165-77. doi: 10.2741/klint.

Abstract

The fibroblast growth factor family, with its prototype members acidic FGF (FGF-1) and basic FGF (FGF-2), binds to four related receptor tyrosine kinases, expressed on most types of cells in tissue culture. In many respects, the FGF receptors appear similar to other growth factor receptors. Thus, dimerization of receptor monomers upon ligand binding is likely to be a requisite for activation of the kinase domains, leading to receptor trans phosphorylation. FGF receptor-1 (FGFR-1), which shows the broadest expression pattern of the four FGF receptors contains at least seven tyrosine phosphorylation sites. A number of signal transduction molecules are affected by binding with different affinities to these phosphorylation sites. The potential roles of these signal transduction molecules in FGF-induced biological responses and in pathological processes are discussed.

Publication types

  • Review

MeSH terms

  • Alternative Splicing
  • Animals
  • Bone Diseases / pathology
  • Cell Physiological Phenomena
  • Dimerization
  • Embryonic and Fetal Development
  • Fibroblast Growth Factors / physiology*
  • Heparan Sulfate Proteoglycans / physiology
  • Humans
  • Neoplasms / pathology
  • Phosphorylation
  • Protein-Tyrosine Kinases / metabolism
  • Receptors, Fibroblast Growth Factor / chemistry
  • Receptors, Fibroblast Growth Factor / genetics
  • Receptors, Fibroblast Growth Factor / metabolism
  • Receptors, Fibroblast Growth Factor / physiology*
  • Signal Transduction
  • src Homology Domains

Substances

  • Heparan Sulfate Proteoglycans
  • Receptors, Fibroblast Growth Factor
  • Fibroblast Growth Factors
  • Protein-Tyrosine Kinases