Regulation of the oncoprotein Smoothened by small molecules

Nat Chem Biol. 2015 Apr;11(4):246-55. doi: 10.1038/nchembio.1776.

Abstract

The Hedgehog pathway is critical for animal development and has been implicated in multiple human malignancies. Despite great interest in targeting the pathway pharmacologically, many of the principles underlying the signal transduction cascade remain poorly understood. Hedgehog ligands are recognized by a unique receptor system that features the transporter-like protein Patched and the G protein-coupled receptor (GPCR)-like Smoothened (SMO). The biochemical interaction between these transmembrane proteins is the subject of intensive efforts. Recent structural and functional studies have provided great insight into the small-molecule regulation of SMO through identification of two distinct ligand-binding sites. In this Perspective, we review these recent findings and relate them to potential mechanisms for the endogenous regulation of SMO.

Publication types

  • Review

MeSH terms

  • Allosteric Site
  • Amino Acid Sequence
  • Animals
  • Cell Membrane / metabolism
  • Drosophila
  • Gene Expression Regulation*
  • Gene Expression Regulation, Neoplastic*
  • Humans
  • Ligands
  • Mice
  • Molecular Conformation
  • Molecular Sequence Data
  • Mutation
  • Neoplasms / genetics
  • Neoplasms / metabolism
  • Patched Receptors
  • Protein Binding
  • Protein Structure, Tertiary
  • Receptors, Cell Surface / genetics
  • Receptors, G-Protein-Coupled / genetics
  • Receptors, G-Protein-Coupled / metabolism*
  • Sequence Homology, Amino Acid
  • Smoothened Receptor
  • Sterols / chemistry
  • Veratrum Alkaloids / chemistry

Substances

  • Ligands
  • Patched Receptors
  • Receptors, Cell Surface
  • Receptors, G-Protein-Coupled
  • SMO protein, human
  • Smoothened Receptor
  • Sterols
  • Veratrum Alkaloids
  • cyclopamine