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Distinct functionality of dishevelled isoforms on Ca2+/calmodulin-dependent protein kinase 2 (CamKII) in Xenopus

Marc Gentzel1, Carolin Schille2, Verena Rauschenberger2

  • 1Max Planck Institute of Molecular Cell Biology and Genetics, 01307 Dresden, Germany.

Molecular Biology of the Cell
|January 9, 2015
PubMed

Insights

Dishevelled (Dvl) and β-arrestin protein complexes dictate specific Wnt signaling pathways. Different Dvl proteins interact with CamKII, modulating distinct Wnt cascades like Wnt/Ca(2+) and convergent extension.

Area of Science:

  • Cellular signaling pathways
  • Molecular biology
  • Developmental biology

Background:

  • Wnt ligands activate diverse intracellular cascades, including β-catenin-dependent and independent pathways.
  • Shared effector proteins like frizzled, dishevelled (Dvl), and β-arrestin are involved in Wnt signaling.
  • Mechanisms for specific Wnt pathway activation and signal integration remain unclear.

Purpose of the Study:

  • To investigate how the composition of dishevelled-β-arrestin protein complexes contributes to Wnt signal specificity.
  • To identify novel interaction partners of the dishevelled-β-arrestin complex.

Main Methods:

  • Quantitative functional proteomics was employed to identify interaction partners.
  • Differential interaction studies between CamKII isoforms and Dvl proteins were performed.
  • Functional studies in Xenopus gastrulation assessed Dvl-mediated CamKII function.

Main Results:

  • CamKII was identified as an interaction partner of the dishevelled-β-arrestin protein complex.
  • Specific CamKII isoforms exhibit differential interactions with Dvl1, Dvl2, and Dvl3.
  • Dvl1 is crucial for CamKII and PKC activation in the Wnt/Ca(2+) pathway; Dvl2 mediates CamKII function downstream of Dvl1 in convergent extension.

Conclusions:

  • The composition of dishevelled-β-arrestin complexes plays a key role in Wnt signal specificity.
  • Differential interactions between Dvl proteins and downstream effectors like CamKII contribute to the activation of distinct Wnt signaling branches.

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