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Smoothened transduces Hedgehog signal by physically interacting with Costal2/Fused complex through its C-terminal tail.

Genes & development

Animals, Signal Transduction, Sequence Deletion, metabolism, genetics, Receptors, G-Protein-Coupled, Protein-Serine-Threonine Kinases, Mutation, Kinesin, Hedgehog Proteins, Drosophila Proteins, physiology, Drosophila

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      Abstract

      The Hedgehog (Hh) family of secreted proteins controls many aspects of growth and patterning in animal development. The seven-transmembrane protein Smoothened (Smo) transduces the Hh signal in both vertebrates and invertebrates; however, the mechanism of its action remains unknown. We found that Smo lacking its C-terminal tail (C-tail) is inactive, whereas membrane-tethered Smo C-tail has constitutive albeit low levels of Hh signaling activity. Smo physically interacts with Costal2 (Cos2) and Fused (Fu) through its C-tail. Deletion of the Cos2/Fu-binding domain from Smo abolishes its signaling activity. Moreover, overexpressing Cos2 mutants that fail to bind Fu and Ci but retain Smo-binding activity blocks Hh signaling. Taken together, our results suggest that Smo transduces the Hh signal by physically interacting with the Cos2/Fu protein complex.

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      Author and article information

      Journal
      14597665
      10.1101/gad.1136603
      280620

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