ArticleScience signaling2019
A direct heterotypic interaction between the DIX domains of Dishevelled and Axin mediates signaling to β-catenin.
Article in Science signaling, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 24 citations in OpenAlex.
- Mutational scanning reveals substrate-assisted autoregulation of the WNT destruction complex.Nature genetics · 2026Article
- Mutational scanning reveals substrate-assisted autoregulation of the WNT destruction complex.bioRxiv : the preprint server for biology · 2025Article
- Wnt signalosome assembly is governed by conformational flexibility of Axin and by the AP2 clathrin adaptor.Nature communications · 2025Article
- Article
- Emerging regulatory mechanisms and functions of biomolecular condensates: implications for therapeutic targets.Signal transduction and targeted therapy · 2025Review
- Review
- Article
- Dishevelled phase separation promotes Wnt signalosome assembly and destruction complex disassembly.The Journal of cell biology · 2022Article
- Nucleation of the destruction complex on the centrosome accelerates degradation of β-catenin and regulates Wnt signal transmission.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- PI(4,5)PScience signaling · 2022Article
- Wnt/β-catenin signaling: Structure, assembly and endocytosis of the signalosome.Development, growth & differentiation · 2021Review
- The structural biology of canonical Wnt signalling.Biochemical Society transactions · 2020Review
- Single-molecule dynamics of Dishevelled at the plasma membrane and Wnt pathway activation.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Wnt regulation: exploring Axin-Disheveled interactions and defining mechanisms by which the SCF E3 ubiquitin ligase is recruited to the destruction complex.Molecular biology of the cell · 2020Article
- Limited dishevelled/Axin oligomerization determines efficiency of Wnt/β-catenin signal transduction.eLife · 2020Article
- Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
Abstract
The Wnt-β-catenin signaling pathway regulates embryonic development and tissue homeostasis throughout the animal kingdom. Signaling through this pathway crucially depends on the opposing activities of two cytoplasmic multiprotein complexes: the Axin destruction complex, which destabilizes the downstream effector β-catenin, and the Dishevelled signalosome, which inactivates the Axin complex and thus enables β-catenin to accumulate and operate a transcriptional switch in the nucleus. These complexes are assembled by dynamic head-to-tail polymerization of the DIX domains of Axin or Dishevelled, respectively, which increases their avidity for signaling effectors. Axin also binds to Dishevelled through its DIX domain. Here, we report the crystal structure of the heterodimeric complex between the two DIX domains of Axin and Dishevelled. This heterotypic interface resembles the interfaces observed in the individual homopolymers, albeit exhibiting a slight rearrangement of electrostatic interactions and hydrogen bonds, consistent with the heterotypic interaction being favored over the homotypic Axin DIX interaction. Last, cell-based signaling assays showed that heterologous polymerizing domains functionally substituted for the DIX domain of Dishevelled provided that these Dishevelled chimeras retained a DIX head or tail surface capable of binding to Axin. These findings indicate that the interaction between Dishevelled and Axin through their DIX domains is crucial for signaling to β-catenin.
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Registered trials
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