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Dishevelled-2 docks and activates Src in a Wnt-dependent manner

Noriko Yokoyama1, Craig C Malbon

  • 1Department of Pharmacology, Health Sciences Center, State University of New York at Stony Brook, Stony Brook, NY 11794-8651, USA. noriko@pharm.stonybrook.edu

Journal of Cell Science
|November 19, 2009
PubMed

Insights

Src tyrosine kinase activity is crucial for Wnt3a-stimulated canonical Wnt/beta-catenin signaling. This pathway regulates gene transcription and primitive endoderm formation, essential for development.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Developmental Biology

Background:

  • The canonical Wnt/beta-catenin signaling pathway is vital for embryonic development.
  • This pathway involves beta-catenin nuclear accumulation and Lef/Tcf-sensitive gene transcription.

Purpose of the Study:

  • To investigate the role of tyrosine kinase activity in Wnt/beta-catenin signaling.
  • To identify specific kinases involved in Wnt3a-mediated signaling.

Main Methods:

  • Utilized totipotent mouse F9 teratocarcinoma cells expressing frizzled-1 (Fz1).
  • Employed tyrosine kinase inhibitors (genistein, PP2) and siRNA-mediated Src knockdown.
  • Investigated protein-protein interactions between Src and dishevelled-2 (Dvl2) using a Y18F mutant.

Main Results:

  • Inhibition of tyrosine kinases (genistein, PP2) and Src knockdown attenuated Wnt3a-stimulated Lef/Tcf transcription and primitive endoderm formation.
  • Src directly binds to dishevelled-2 (Dvl2) and is activated by Wnt3a.
  • Dvl2 and beta-catenin were identified as key substrates for tyrosine phosphorylation in this pathway.

Conclusions:

  • Src acts as a positive regulator in the canonical Wnt/beta-catenin signaling pathway.
  • Src-mediated tyrosine phosphorylation of Dvl2 and beta-catenin is essential for Wnt3a-induced developmental gene transcription.

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