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Related Experiment Videos

Mapping sonic hedgehog-receptor interactions by steric interference.

R B Pepinsky1, P Rayhorn, E S Day

  • 1Biogen, Inc., Cambridge, Massachusetts 02142, USA.

The Journal of Biological Chemistry
|February 7, 2001
PubMed
Summary
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Researchers identified key regions on the Sonic hedgehog (Shh) protein crucial for binding its Patched (Ptc) receptor. Modifying specific surface areas revealed critical interaction sites, advancing our understanding of Shh signaling pathways.

Area of Science:

  • Molecular Biology
  • Developmental Biology
  • Biochemistry

Background:

  • Sonic hedgehog (Shh) is a crucial signaling molecule in embryonic development.
  • Patched (Ptc) is the primary receptor for Shh.
  • Understanding Shh-Ptc interactions is vital for developmental biology and disease research.

Purpose of the Study:

  • To map the functional regions of the Shh protein involved in Patched (Ptc) receptor binding.
  • To identify specific amino acid residues critical for Shh-Ptc interaction.
  • To investigate the structural basis of Shh signaling.

Main Methods:

  • Site-directed mutagenesis of surface amino acid residues in Shh to cysteine.
  • Chemical modification of cysteine residues with thiol-specific probes of varying sizes.

Related Experiment Videos

  • Assay of modified Shh protein for Ptc receptor binding activity.
  • Assessment of Shh-induced osteoblast differentiation in C3H10T1/2 cells.

    • Main Results:

    • Approximately one-third of the Shh surface can be modified without affecting function.
    • Specific residues (Asn-50, Ser-156) are highly sensitive to modification, indicating proximity to the Ptc-binding site.
    • Shh-Ptc interaction is mediated by a large surface area of the Shh protein.
    • The epitope for the neutralizing antibody 5E1 is located near, but distinct from, the Ptc-binding site.

    Conclusions:

    • The study defines critical regions on the Shh protein for Ptc receptor binding.
    • Structure-activity relationship data provide novel insights into Shh-Ptc interactions.
    • These findings enhance the understanding of Shh pathway regulation in development and disease.