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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
Summary
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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