ArticleStructure (London, England : 1993)2017
Regulation of Receptor Binding Specificity of FGF9 by an Autoinhibitory Homodimerization.
Article in Structure (London, England : 1993), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
22 citing papers in PubMed, 36 citations in OpenAlex.
- Reprogramming FGFR isoform specificity in FGF2 by deep mutational scanning.Chemical science · 2026Article
- N-terminal helix formation and dimer-monomer transition of FGF10 in specific recognition of FGFR2b.The FEBS journal · 2025Article
- Fibroblast Growth Factor-Derived Peptides: Sources, Functions, and Applications.Bioengineering (Basel, Switzerland) · 2025Review
- FGF-based drug discovery: advances and challenges.Nature reviews. Drug discovery · 2025Review
- GPNMB is a novel binding partner of FGFR1 that affects tumorigenic potential through AKT phosphorylation in TNBC.Cancer science · 2025Article
- Short-range Fgf signalling patterns hindbrain progenitors to induce the neurogenesis-to-oligodendrogenesis switch.Development (Cambridge, England) · 2024Article
- Fgf9 promotes incisor dental epithelial stem cell survival and enamel formation.Stem cell research & therapy · 2024Article
- Article
- Engineered FGF19BMC biotechnology · 2023Article
- NMR resonance assignment of a fibroblast growth factor 8 splicing isoform b.Biomolecular NMR assignments · 2023Article
- Structural basis for FGF hormone signalling.Nature · 2023Article
- New developments in the biology of fibroblast growth factors.WIREs mechanisms of disease · 2022Review
- Characterization of clostridium botulinum neurotoxin serotype A (BoNT/A) and fibroblast growth factor receptor interactions using novel receptor dimerization assay.Scientific reports · 2021Article
- A novel heterozygous variant in FGF9 associated with previously unreported features of multiple synostosis syndrome 3.Clinical genetics · 2021Article
- Curtailing FGF19's mitogenicity by suppressing its receptor dimerization ability.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Fibroblast growth factor signalling in osteoarthritis and cartilage repair.Nature reviews. Rheumatology · 2020Review
- Interaction of FGF9 with FGFR3-IIIb/IIIc, a putative driver of growth and aggressive behaviour of hepatocellular carcinoma.Liver international : official journal of the International Association for the Study of the Liver · 2020Article
- FGF Pyramus Has a Transmembrane Domain and Cell-Autonomous Function in Polarity.Current biology : CB · 2020Article
- FGF6 and FGF9 regulate UCP1 expression independent of brown adipogenesis.Nature communications · 2020Article
- Synergistic effects of laminin-1 peptides, VEGF and FGF9 on salivary gland regeneration.Acta biomaterialia · 2019Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
The epithelial fibroblast growth factor 9 (FGF9) subfamily specifically binds and activates the mesenchymal "c" splice isoform of FGF receptors 1-3 (FGFR1-3) to regulate organogenesis and tissue homeostasis. The unique N and C termini of FGF9 subfamily ligands mediate a reversible homodimerization that occludes major receptor binding sites within the ligand core region. Here we provide compelling X-ray crystallographic, biophysical, and biochemical data showing that homodimerization controls receptor binding specificity of the FGF9 subfamily by keeping the concentration of active FGF9 monomers at a level, which is sufficient for a normal FGFR "c" isoform binding/signaling, but is insufficient for an illegitimate FGFR "b" isoform binding/signaling. We show that deletion of the N terminus or alanine substitutions in the C terminus of FGF9 skews the delicate ligand equilibrium toward active FGF9 monomers causing off-target binding and activation of FGFR b isoforms. Our study is the first to implicate ligand homodimerization in the regulation of ligand-receptor specificity.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.