Fibroblast growth factor receptor-4 shows novel features in genomic structure, ligand binding and signal transduction.

Research Article1 December 1992free access Fibroblast growth factor receptor-4 shows novel features in genomic structure, ligand binding and signal transduction. S. Vainikka S. Vainikka Department of Pathology, University of Helsinki, Finland. Search for more papers by this author J. Partanen J. Partanen Department of Pathology, University of Helsinki, Finland. Search for more papers by this author P. Bellosta P. Bellosta Department of Pathology, University of Helsinki, Finland. Search for more papers by this author F. Coulier F. Coulier Department of Pathology, University of Helsinki, Finland. Search for more papers by this author D. Birnbaum D. Birnbaum Department of Pathology, University of Helsinki, Finland. Search for more papers by this author C. Basilico C. Basilico Department of Pathology, University of Helsinki, Finland. Search for more papers by this author M. Jaye M. Jaye Department of Pathology, University of Helsinki, Finland. Search for more papers by this author K. Alitalo K. Alitalo Department of Pathology, University of Helsinki, Finland. Search for more papers by this author S. Vainikka S. Vainikka Department of Pathology, University of Helsinki, Finland. Search for more papers by this author J. Partanen J. Partanen Department of Pathology, University of Helsinki, Finland. Search for more papers by this author P. Bellosta P. Bellosta Department of Pathology, University of Helsinki, Finland. Search for more papers by this author F. Coulier F. Coulier Department of Pathology, University of Helsinki, Finland. Search for more papers by this author D. Birnbaum D. Birnbaum Department of Pathology, University of Helsinki, Finland. Search for more papers by this author C. Basilico C. Basilico Department of Pathology, University of Helsinki, Finland. Search for more papers by this author M. Jaye M. Jaye Department of Pathology, University of Helsinki, Finland. Search for more papers by this author K. Alitalo K. Alitalo Department of Pathology, University of Helsinki, Finland. Search for more papers by this author Author Information S. Vainikka1, J. Partanen1, P. Bellosta1, F. Coulier1, D. Birnbaum1, C. Basilico1, M. Jaye1 and K. Alitalo1 1Department of Pathology, University of Helsinki, Finland. The EMBO Journal (1992)11:4273-4280https://doi.org/10.1002/j.1460-2075.1992.tb05526.x Correction(s) for this article Corrigendum01 February 1993 PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info Fibroblast growth factor (FGF) receptor (FGFR) gene family consists of at least four receptor tyrosine kinases that transduce signals important in a variety of developmental and physiological processes related to cell growth and differentiation. Here we have characterized the binding of different FGFs to FGFR-4. Our results establish an FGF binding profile for FGFR-4 with aFGF having the highest affinity, followed by K-FGF/hst-1 and bFGF. In addition, FGF-6 was found to bind to FGFR-4 in ligand competition experiments. Interestingly, the FGFR-4 gene was found to encode only the prototype receptor in a region where both FGFR-1 and FGFR-2 show alternative splicing leading to differences in their ligand binding specificities and to secreted forms of these receptors. Ligands binding to FGFR-4 induced receptor autophosphorylation and phosphorylation of a set of cellular polypeptides, which differed from those phosphorylated in FGFR-1-expressing cells. Specifically, the FGFR-1-expressing cells showed a considerably more extensive tyrosine phosphorylation of PLC-gamma than the FGFR-4-expressing cells. Structural and functional specificity within the FGFR family exemplified by FGFR-4 may help to explain how FGFs perform their diverse functions. Previous ArticleNext Article Volume 11Issue 121 December 1992In this issue RelatedDetailsLoading ...