All Dact (Dapper/Frodo) scaffold proteins dimerize and exhibit conserved interactions with Vangl, Dvl, and serine/threonine kinases
2011

Dact Proteins and Their Role in Cell Signaling

publication Evidence: moderate

Author Information

Author(s): Kivimäe Saul, Yang Xiao Yong, Cheyette Benjamin NR

Primary Institution: The Nina Ireland Laboratory of Developmental Neurobiology, Department of Psychiatry, University of California San Francisco

Hypothesis

Distinct protein-protein interactions confer distinct signaling activities onto each Dact paralog.

Conclusion

Dact proteins play a conserved role in kinase-regulated biochemistry involving Vangl and Dvl, suggesting their involvement in the Planar Cell Polarity pathway.

Supporting Evidence

  • All Dact paralogs form complexes with Vangl and Dvl proteins.
  • Dact proteins dimerize through their conserved leucine zipper domains.
  • Interactions with kinases like CK1δ/ε, PKA, and PKC are conserved across Dact family members.
  • Complex formation with catenin proteins is relatively weak but conserved for p120ctn.

Takeaway

Dact proteins are like helpers in a team that work together to send important signals in cells, helping them know where to go and how to behave.

Methodology

The study involved co-immunoprecipitation assays to analyze protein complex formation in human embryonic kidney cells.

Limitations

The study primarily focused on murine models, which may not fully represent human biology.

Digital Object Identifier (DOI)

10.1186/1471-2091-12-33

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