FIBROBLAST GROWTH FACTOR RECEPTOR

The 'fibroblast growth factor receptors' are, as their name implies, receptors which bind to members of the fibroblast growth factor family of proteins.

Contents

Structure

Genes

References

Structure

The fibroblast growth factor receptors consist of an extracellular ligand domain comprised of three immunoglobulin-like domains, a single transmembrane helix domain, and an intracellular domain with tyrosine kinase activity.
The fibroblast growth factors are the largest family of growth factor ligands comprising of 23 members. Fibroblast growth factors, Ornitz DM. and Itoh, N., , , Genome Biol., 2001
The natural alternate splicing of four fibroblast growth factor receptor (FRFR) genes results in the production of over 48 different isoforms of FGFR. N-glycosylation of fibroblast growth factor receptor 1 regulates ligand and heparan sulfate co-receptor binding, Duchesne L, Tissot B. ''et al'', , , J. Biol. Chem., 2006
These isoforms vary in their ligand binding properties and kinase domains, however all share the common extracellular region composed of three immunoglobulin (Ig) like domains (D1-D3), and thus belong to the immunoglobulin superfamily. Receptors for fibroblast growth factors, Coutts JC, and Gallagher JT., , , Immunol. Cell. Biol., 1995
The three immunoglobin(Ig)-like domains, D1, D2 and D3, present a stretch of acidic amino acids ("the acidic box") between D1 and D2. This "acidic box" can participate in the regulation of FGF binding to the FGFR. Immunoglobulin-like domains D2 and D3 are sufficient for FGF binding. Each receptor can be activated by several FGFs. In many cases the FGFs themselves can also activate more than one receptor, this is not the case with FGF-7 however which can only activate FGFR2b.
A gene for a fifth FGFR protein, FGFR5, has also been identified. In contrast to FGFRs 1-4 it lacks a cytoplasmic tyrosine kinase domain and one isoform, FGFR5γ, only contains the extracellular domains D1 and D2. Identification of a new fibroblast growth factor receptor, FGFR5, Sleeman M, Fraser J. ''et al'', , , Gene, 2001
The FGFRs are known to dimerize as heterodimers and homodimers.

Genes

So far, five distinct membrane FGFR have been identified in vertebrates and all of them belong to the tyrosine kinase superfamily (FGFR1 to FGFR4).

★ (see also Fibroblast growth factor receptor 1)

★ (see also Fibroblast growth factor receptor 2)

★ (see also Fibroblast growth factor receptor 3)

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References