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• W2737639666 endingPage "1336.e3" @default.
• W2737639666 startingPage "1325" @default.
• W2737639666 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." @default.
• W2737639666 created "2017-07-31" @default.
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• W2737639666 date "2017-09-01" @default.
• W2737639666 modified "2023-10-12" @default.
• W2737639666 title "Regulation of Receptor Binding Specificity of FGF9 by an Autoinhibitory Homodimerization" @default.
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• W2737639666 doi "https://doi.org/10.1016/j.str.2017.06.016" @default.
• W2737639666 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5587394" @default.
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