Nanoscale organization of hedgehog is essential for long-range signaling

Cell. 2008 Jun 27;133(7):1214-27. doi: 10.1016/j.cell.2008.05.026.

Abstract

Hedgehog (Hh) plays crucial roles in tissue-patterning and activates signaling in Patched (Ptc)-expressing cells. Paracrine signaling requires release and transport over many cell diameters away by a process that requires interaction with heparan sulfate proteoglycans (HSPGs). Here, we examine the organization of functional, fluorescently tagged variants in living cells by using optical imaging, FRET microscopy, and mutational studies guided by bioinformatics prediction. We find that cell-surface Hh forms suboptical oligomers, further concentrated in visible clusters colocalized with HSPGs. Mutation of a conserved Lys in a predicted Hh-protomer interaction interface results in an autocrine signaling-competent Hh isoform--incapable of forming dense nanoscale oligomers, interacting with HSPGs, or paracrine signaling. Thus, Hh exhibits a hierarchical organization from the nanoscale to visible clusters with distinct functions.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Body Patterning
  • Cell Membrane / chemistry
  • Cell Membrane / metabolism
  • Drosophila melanogaster / chemistry
  • Drosophila melanogaster / embryology
  • Drosophila melanogaster / metabolism*
  • Fluorescence Resonance Energy Transfer
  • Green Fluorescent Proteins / chemistry
  • Green Fluorescent Proteins / metabolism
  • Hedgehog Proteins / chemistry*
  • Hedgehog Proteins / genetics
  • Hedgehog Proteins / metabolism*
  • Heparan Sulfate Proteoglycans / metabolism
  • Mutation
  • Protein Structure, Tertiary
  • Recombinant Fusion Proteins / chemistry
  • Recombinant Fusion Proteins / genetics
  • Recombinant Fusion Proteins / metabolism
  • Signal Transduction*

Substances

  • Hedgehog Proteins
  • Heparan Sulfate Proteoglycans
  • Recombinant Fusion Proteins
  • Green Fluorescent Proteins