Receptor Specificity of the Fibroblast Growth Factor Family*

  title={Receptor Specificity of the Fibroblast Growth Factor Family*},
  author={David M. Ornitz and Jingsong Xu and Jennifer S. Colvin and Donald G. McEwen and Craig A. MacArthur and François Coulier and Guang Gao and Mitchell Goldfarb},
  journal={The Journal of Biological Chemistry},
  pages={15292 - 15297}
Fibroblast growth factors (FGFs) are essential molecules for mammalian development. The nine known FGF ligands and the four signaling FGF receptors (and their alternatively spliced variants) are expressed in specific spatial and temporal patterns. The activity of this signaling pathway is regulated by ligand binding specificity, heparan sulfate proteoglycans, and the differential signaling capacity of individual FGF receptors. To determine potentially relevant ligand-receptor pairs we have… 

Figures and Tables from this paper

Receptor Specificity of the Fibroblast Growth Factor Family
This study completes the mitogenesis-based comparison of receptor specificity of the entire FGF family under standard conditions and should help in interpreting and predicting in vivo biological activity.
Signal transduction by fibroblast growth factor receptors.
Dimmerization of receptor monomers upon ligand binding is likely to be a requisite for activation of the kinase domains, leading to receptor trans phosphorylation, and the potential roles of these signal transduction molecules in FGF-induced biological responses and in pathological processes are discussed.
Fibroblast growth factors and their receptors in the central nervous system
Fibroblast growth factors and their receptors constitute an elaborate signaling system that participates in many developmental and repair processes of virtually all mammalian tissues and are major determinants of neuronal survival both during development and during adulthood.
Fibroblast growth factors, their receptors and signaling.
FGF signaling also appears to play a role in tumor growth and angiogenesis, and autocrine FGF signaling may be particularly important in the progression of steroid hormone-dependent cancers to a hormone-independent state.
Molecular characteristics of fibroblast growth factor-fibroblast growth factor receptor-heparin-like glycosaminoglycan complex.
It is proposed that the FGF-FGFR interaction mediated by the 'conserved' primary site interactions is likely to be similar if not identical for the entire FGF family, whereas the 'variable' secondary sites, on both FGF as well as FGFR mediates specificity of a given FGF to a given FGFR isoform.
Isoforms of Receptors of Fibroblast Growth Factors
  • S. Gong
  • Biology
    Journal of cellular physiology
  • 2014
A better understanding of the diversity of FGF signaling in different developmental contexts and diseased states can be achieved through increased knowledge of the presence of specific FGFR isoforms and their impact on downstream signaling and functions.
Structural basis for fibroblast growth factor receptor activation.
Fibroblast growth factor receptors and their ligands in the adult rat kidney.
The distributions of the FGFRs in the normal adult kidney and the restricted expression of FGF ligands suggest that specific FGFs have distinct and important roles in the maintenance of normal kidney structure and function.


Expression and Biological Activity of Mouse Fibroblast Growth Factor-9 (*)
FGF-9 binds to and activates the “b” splice form of FGFR3, thus becoming the first FGF ligand besides FGF-1 to activate this highly specific member of the FGF receptor family.
Fibroblast growth factor receptor‐4 shows novel features in genomic structure, ligand binding and signal transduction.
An FGF binding profile for FGFR‐4 is established with aFGF having the highest affinity, followed by K‐FGF/hst‐1 and bFGF, and FGF‐6 was found to bind to FGFR•4 in ligand competition experiments.
Fibroblast growth factor receptors have different signaling and mitogenic potentials.
Compared the properties of BaF3 murine lymphoid cells and L6 rat myoblast cells engineered to express FGFR-1 orFGFR-4 are compared, finding that the signaling and biological responses elicited by different FGF receptors substantially differ.
Fibroblast growth factor receptor (FGFR) 3. Alternative splicing in immunoglobulin-like domain III creates a receptor highly specific for acidic FGF/FGF-1.
It is demonstrated both by binding studies on genetically engineered soluble receptors and by the mitogenic response of growth factor-dependent cell lines that this splice variant of FGFR3 (FGFR3 IIIb), by binding only acidic FGF (aFGF/FGF-1), has the most restricted ligand binding properties of any FGFR thus far described.
Receptor Binding and Mitogenic Properties of Mouse Fibroblast Growth Factor 3
A comparison of two mammary epithelial cell lines showed a marked difference of potency and dependence upon heparin in their response to mouse Fgf3, suggesting a complex interaction between the ligand and its low and high affinity receptors.