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Sonic hedgehog multimerization: a self-organizing event driven by post-translational modifications?

Mirella V Koleva1,2,3,4, Stephen Rothery5, Martin Spitaler5

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|August 28, 2015
PubMed
Summary
This summary is machine-generated.

Sonic hedgehog (Shh) protein travels extracellularly by forming large, self-assembled multimers. Lipid modifications like cholesterol and palmitate influence Shh multimer size and shape, impacting its developmental roles.

Keywords:
CholesterylShhhomomultimerizationpalmitoylself-assembly

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Area of Science:

  • Biochemistry
  • Developmental Biology
  • Cell Biology

Background:

  • Sonic hedgehog (Shh) is a crucial morphogen in development and homeostasis.
  • Pathway dysregulation is linked to carcinogenesis.
  • Shh's lipophilic nature and extracellular transport mechanism remain poorly understood.

Purpose of the Study:

  • To elucidate the mechanism of Sonic hedgehog (Shh) multimer assembly and release.
  • To investigate the role of lipid modifications in Shh multimerization.
  • To understand how Shh achieves extracellular transport.

Main Methods:

  • High-resolution optical imaging.
  • Utilized post-translational modification mutants of Shh.
  • Analyzed Shh cluster dimensions and release kinetics.

Main Results:

  • C-terminal cholesterol and N-terminal palmitate adducts promote large Shh multimer assembly and regulate their shape.
  • Small Shh multimers form even without lipid modifications.
  • Multimerization is driven by self-assembly following the law of mass action.

Conclusions:

  • Shh multimerization is a self-assembly process.
  • Lipid modifications enhance Shh multimer size by increasing membrane association.
  • Understanding Shh transport is key to its role in development and disease.