Open Access
Article
Signal transduction by fibroblast growth factor receptors
P Klint1,L Claesson-Welsh1
1
Dept. of Med. Biochemistry and Microbiology, Biomedical Center, Box 575, S-751 23 Uppsala, Sweden
DOI: 10.2741/klint Volume 4 Issue 4, pp.165-177
Published: 15 February 1999
(This article belongs to the Special Issue Signaling through protein kinase C)
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.

Share and Cite
P Klint, L Claesson-Welsh. Signal transduction by fibroblast growth factor receptors. Frontiers in Bioscience-Landmark. 1999. 4(4); 165-177.