Structural basis of the recognition of the Dishevelled DEP domain in the Wnt signaling pathway

@article{Wong2000StructuralBO,
  title={Structural basis of the recognition of the Dishevelled DEP domain in the Wnt signaling pathway},
  author={Hing C. Wong and Junhao Mao and Jason T. Nguyen and Shamala K Srinivas and Weixing Zhang and Bo Liu and Lin Li and Dianqing Wu and Jie Zheng},
  journal={Nature Structural Biology},
  year={2000},
  volume={7},
  pages={1178-1184}
}
The DEP domain of Dishevelled (Dvl) proteins transduces signals to effector proteins downstream of Dvl in the Wnt pathway. Here we report that DEP-containing mutants inhibit Wnt-induced, but not Dvl-induced, activation of the transcription factor Lef-1. This inhibitory effect is weakened by a K434M mutation. Nuclear magnetic resonance spectroscopy revealed that the DEP domain of mouse Dvl1 comprises a three-helix bundle, a β-hairpin `arm' and two short β-strands at the C-terminal region. Lys… CONTINUE READING

From This Paper

Figures, tables, and topics from this paper.
30 Citations
60 References
Similar Papers

Citations

Publications citing this paper.
Showing 1-10 of 30 extracted citations

References

Publications referenced by this paper.
Showing 1-10 of 60 references

Similar Papers

Loading similar papers…