ArticleChembiochem : a European journal of chemical biology2025
Developing FGF2 Mutants with Selectively Reduced Heparan Sulfate Affinity to Explore their Impact on FGFR1 Signaling.
Article in Chembiochem : a European journal of chemical biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed.
- Reprogramming FGFR isoform specificity in FGF2 by deep mutational scanning.Chemical science · 2026Article
- Structure-function relationship in FGF signaling: rational design of highly stable FGF2 variants and their effect on cell growth, metabolism, and survival.Journal of biological engineering · 2026Article
- Developing FGF2 Mutants with Selectively Reduced Heparan Sulfate Affinity to Explore their Impact on FGFR1 Signaling.Chembiochem : a European journal of chemical biology · 2025Article
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6 authors.
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Abstract
Fibroblast growth factor 2 (FGF2)regulates signal transduction by forming complexes with its receptors, FGF receptors (FGFRs), and heparan sulfate (HS), playing a crucial role in biological systems. Although HS has been suggested to modulate FGF/FGFR signaling as a coreceptor, multiple hypotheses exist regarding how HS affects FGF/FGFR signaling and the mechanism remains unclear. Herein, to highlight the role of FGF2/HS interaction in FGF2/FGFR1 signaling, FGF2 mutants with reduced HS-binding affinity are rationally designed through in silico analysis. These FGF2 mutants exhibit reduced HS affinity by more than two orders of magnitude while maintaining binding affinity to FGFR1. In addition, these mutants retain their thermal stability. Cellular assays using the FGF2 mutant suggest that, contrary to previous reports, the contribution of the FGF2/HS interaction in FGF2/FGFR1 signaling may be limited. The mutant FGFs that specifically alter the interaction with HS, achieved in this study, would contribute to an understanding of the role of FGF/HS interaction in FGF/FGFR signaling.
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