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Article

Structural basis of the recognition of the dishevelled DEP domain in the Wnt signaling pathway.

Nature structural biology - 1 Dec 2000

Wong H C, Mao J, Nguyen J T, Srinivas S, Zhang W, Liu B, Li L, Wu D, Zheng J

Abstract excerpt

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...

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Identifiers

PMID: 11101902
DOI: 10.1038/82047
PMCID: PMC4381838

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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