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Integration of the beta-catenin-dependent Wnt pathway with integrin signaling through the adaptor molecule Grb2

Steve P Crampton1, Beibei Wu, Edward J Park

  • 1Department of Molecular Biology and Biochemistry, UCI Institute for Immunology, University of California Irvine, Irvine, California, USA.

Plos One
|November 20, 2009
PubMed
Abstract

Insights

The adapter protein Grb2 modifies beta-catenin-dependent Wnt signaling. Integrin ligation and FAK activation synergize with Wnt signaling via a Grb2-rac-jnk-c-jun pathway, offering context-dependent Wnt modulation.

Area of Science:

  • Cellular signaling pathways
  • Molecular biology
  • Signal transduction

Background:

  • Wnt signaling complexity arises from multiple Frizzled receptor pathways and context-dependent signals.
  • Upstream activators for rac1 and c-jun in Wnt signaling remain unidentified.

Purpose of the Study:

  • To identify upstream activators of rac1 and c-jun in Wnt signaling.
  • To elucidate the role of the adapter protein Grb2 in Wnt signaling.

Main Methods:

  • Utilized reporter assays to assess Wnt signaling activity.
  • Employed dominant-negative constructs and siRNA to inhibit Grb2 function.
  • Investigated the impact of integrin ligation and Focal Adhesion Kinase (FAK) on Wnt signaling.

Main Results:

  • Identified Grb2 as a modifier of beta-catenin-dependent Wnt signaling.
  • Demonstrated that Grb2, rac1, JNK, and c-jun mediate Wnt signaling.
  • Showed that integrin ligation and FAK activation synergize with Wnt signaling through a Grb2-dependent pathway.

Conclusions:

  • Wnt signaling is modulated by a Grb2-rac-jnk-c-jun pathway.
  • Integrin ligation and FAK activation provide context-dependent synergy with Wnt signaling.

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