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Related Experiment Videos

Structural basis for fibroblast growth factor receptor activation.

Moosa Mohammadi1, Shaun K Olsen, Omar A Ibrahimi

  • 1Department of Pharmacology, New York University School of Medicine, 550 First Avenue, MSB 425, New York, NY 10016, USA. mohammad@saturn.med.nyu.edu

Cytokine & Growth Factor Reviews
|May 3, 2005
PubMed
Summary

Fibroblast Growth Factor (FGF) signaling regulates development and homeostasis but aberrant signaling causes disease. This review clarifies FGF-FGFR dimerization mechanisms using structural and biochemical studies, highlighting pathogenic mutations.

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Area of Science:

  • Molecular Biology
  • Structural Biology
  • Biochemistry

Background:

  • Fibroblast Growth Factor (FGF) signaling is crucial for embryonic development, homeostasis, and regeneration.
  • Dysregulated FGF signaling is implicated in various human pathologies, including skeletal disorders, metabolic diseases, and cancer.
  • FGFs interact with cell surface Fibroblast Growth Factor Receptors (FGFRs), requiring precise binding specificity for proper function.

Purpose of the Study:

  • To review recent structural and biochemical studies on FGF-FGFR dimerization and binding specificity.
  • To differentiate between competing crystallographic models of FGFR dimerization.
  • To elucidate the molecular mechanisms underlying FGF-FGFR interactions and the role of heparin/heparan sulfate (HS).

Main Methods:

Related Experiment Videos

  • Analysis of recent crystallographic data for FGF-FGFR complexes.
  • Biochemical and biophysical studies investigating FGF-FGFR dimerization.
  • Examination of pathogenic FGFR mutations to understand binding specificity mechanisms.

    • Main Results:

    • Two distinct models for FGFR dimerization exist, differing in stoichiometry, heparin requirements, and quaternary structure.
    • Structural and biophysical analyses provide evidence to differentiate these models.
    • Pathogenic FGFR mutations offer critical insights into the precise mechanisms of FGF-FGFR binding and specificity.

    Conclusions:

    • Structural insights into FGF-FGFR complexes clarify mechanisms of binding specificity and promiscuity.
    • Understanding these interactions explains the molecular basis of craniosynostosis and other skeletal disorders.
    • Accurate FGF-FGFR dimerization is essential for normal biological processes and preventing disease.