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Interaction between Smad 3 and Dishevelled in murine embryonic craniofacial mesenchymal cells

D R Warner1, R M Greene, M M Pisano

  • 1Department of Molecular, Cellular, and Craniofacial Biology, University of Louisville Birth Defects Center, Louisville, KY 40292, USA.

Orthodontics & Craniofacial Research
|May 13, 2005
PubMed
Abstract

Insights

Smad 3 protein interacts with all three Dishevelled isoforms in vitro and specifically with Dishevelled-1 in vivo. Transforming growth factor beta (TGF-β) signaling enhances this Smad 3 and Dishevelled-1 interaction.

Area of Science:

  • Molecular Biology
  • Cell Signaling

Background:

  • Smad 3 is a key mediator of transforming growth factor beta (TGF-β) signaling.
  • Dishevelled proteins are crucial in Wnt signaling pathways.
  • Interactions between TGF-β and Wnt pathways are increasingly recognized.

Purpose of the Study:

  • To investigate the in vivo interaction between Smad 3 and Dishevelled-1.
  • To determine if Smad 3 interacts with other Dishevelled isoforms.

Main Methods:

  • Cell culture and transfection with myc-Smad 3.
  • Immunoprecipitation using specific antibodies against Dishevelled.
  • Western blotting to detect Smad 3 in Dishevelled immunoprecipitates.
  • Glutathione-S-transferase (GST) pull-down assays.

Main Results:

  • Smad 3 binds to Dishevelled isoforms -1, -2, and -3 in GST pull-down assays.
  • Smad 3 directly interacts with Dishevelled-1 in vivo.
  • Activation of the TGF-β pathway increases the in vivo binding affinity between Smad 3 and Dishevelled-1.

Conclusions:

  • Smad 3 interacts with all known Dishevelled isoforms.
  • The interaction between Smad 3 and Dishevelled-1 occurs in vivo.
  • Transforming growth factor beta (TGF-β) signaling modulates the Smad 3-Dishevelled-1 interaction, suggesting cross-talk between signaling pathways.

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