ArticleProtein science : a publication of the Protein Society2006
Elucidation of the mechanism of the regulatory function of the Ig1 module of the fibroblast growth factor receptor 1.
Article in Protein science : a publication of the Protein Society, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 30 citations in OpenAlex.
- Specific inhibition of fibroblast growth factor receptor 1 signaling by a DNA aptamer.Molecular therapy. Nucleic acids · 2025Article
- FGFR1 clustering with engineered tetravalent antibody improves the efficiency and modifies the mechanism of receptor internalization.Molecular oncology · 2020Article
- FGF2: a novel druggable target for glioblastoma?Expert opinion on therapeutic targets · 2020Review
- Review
- Review
- Nectin-1 binds and signals through the fibroblast growth factor receptor.The Journal of biological chemistry · 2012Article
- Structure of the activating IL-1 receptor signaling complex.Nature structural & molecular biology · 2012Article
- The alternatively spliced acid box region plays a key role in FGF receptor autoinhibition.Structure (London, England : 1993) · 2012Article
- Influence of heparin mimetics on assembly of the FGF.FGFR4 signaling complex.The Journal of biological chemistry · 2010Article
- Fibroblast growth factor receptor-1 phosphorylation requirement for cardiomyocyte differentiation in murine embryonic stem cells.Journal of cellular and molecular medicine · 2009Article
- Structural basis for the activation of FGFR by NCAM.Protein science : a publication of the Protein Society · 2008Article
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The extracellular part of the fibroblast growth factor (FGF) receptor (FGFR) consists of up to three Ig modules (Ig1-Ig3), in which the Ig2 and Ig3 modules determine affinity and specificity for FGF and heparin. The FGFR isoforms lacking the Ig1 module have higher affinity for FGF and heparin than the triple Ig-module isoforms, suggesting that the Ig1 module is involved in the regulation of the FGFR-ligand interaction. We show here by surface plasmon resonance and NMR analyses that the Ig1 module binds to the Ig2 module, and identify by NMR the binding sites involved in the Ig1-Ig2 interaction. The identified binding site in the Ig2 module was found to be in the area of the FGF-Ig2 and Ig2-heparin contact sites, thus providing direct structural evidence that the Ig1 module functions as a competitive autoinhibitor of the FGFR-ligand interaction. Furthermore, the Ig1 binding site of the Ig2 module overlaps the Ig2-Ig2 contact site. This suggests that the function of the Ig1 module is not only regulation of the FGFR-ligand binding affinity but also prevention of spontaneous FGFR dimerization (through a direct Ig2-Ig2 interaction) in the absence of FGF.
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