ArticleThe Journal of biological chemistry2011
Molecular basis of Wnt activation via the DIX domain protein Ccd1.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 46 citations in OpenAlex.
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- Cluster assembly dynamics drive fidelity of planar cell polarity polarization.Nature communications · 2026Article
- Dishevelled localization and function are differentially regulated by structurally distinct sterols.iScience · 2025Article
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- AXIN2 germline testing in a French cohort validates pathogenic variants as a rare cause of predisposition to colorectal polyposis and cancer.Genes, chromosomes & cancer · 2023Article
- Quantitative trait loci on chromosomes 9 and 19 modulate AII amacrine cell number in the mouse retina.Frontiers in neuroscience · 2023Article
- LncRNAs ENST00000499459 and TCONS_00004989 enhance asthma progression in children with house dust mite-induced allergic asthma.Allergy, asthma, and clinical immunology : official journal of the Canadian Society of Allergy and Clinical Immunology · 2022Article
- DIX domain containing 1 (DIXDC1) modulates VEGFR2 level in vasculatures to regulate embryonic and postnatal retina angiogenesis.BMC biology · 2022Article
- The role of the WNT signaling pathway in the maxillary sinus squamous cell carcinoma.Medical oncology (Northwood, London, England) · 2022Article
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- Whole Genome Level Analysis of the Wnt and DIX Gene Families in Mice and Their Coordination Relationship in Regulating Cardiac Hypertrophy.Frontiers in genetics · 2021Article
- The structural biology of canonical Wnt signalling.Biochemical Society transactions · 2020Review
- Limited dishevelled/Axin oligomerization determines efficiency of Wnt/β-catenin signal transduction.eLife · 2020Article
- Article
- A direct heterotypic interaction between the DIX domains of Dishevelled and Axin mediates signaling to β-catenin.Science signaling · 2019Article
- High-resolution structure of a Y27W mutant of the Dishevelled2 DIX domain.Acta crystallographica. Section F, Structural biology communications · 2019Article
- DIXDC1 contributes to psychiatric susceptibility by regulating dendritic spine and glutamatergic synapse density via GSK3 and Wnt/β-catenin signaling.Molecular psychiatry · 2018Article
- Molecular regulation and pharmacological targeting of the β-catenin destruction complex.British journal of pharmacology · 2017Review
- Structural basis for Ccd1 auto-inhibition in the Wnt pathway through homomerization of the DIX domain.Scientific reports · 2017Article
- Downregulated expression of DIXDC1 in hepatocellular carcinoma and its correlation with prognosis.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2016Article
Corrections and comments
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Authors and funding
10 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Wnt signaling plays pivotal roles in embryogenesis and cancer, and the three DIX domain-containing proteins, Dvl, Axin, and Ccd1, play distinct roles in the initiation and regulation of canonical Wnt signaling. Overexpressed Dvl has a tendency to form large polymers in a cytoplasmic punctate pattern, whereas the biologically active Dvl in fact forms low molecular weight oligomers. The molecular basis for how the polymeric sizes of Dvl proteins are controlled upon Wnt signaling remains unclear. Here we show that Ccd1 up-regulates canonical Wnt signaling via acting synergistically with Dvl. We determined the crystal structures of wild type Ccd1-DIX and mutant Dvl1-DIX(Y17D), which pack into "head-to-tail" helical filaments. Structural analyses reveal two sites crucial for intra-filament homo- and hetero-interaction and a third site for inter-filament homo-assembly. Systematic mutagenesis studies identified critical residues from all three sites required for Dvl homo-oligomerization, puncta formation, and stimulation of Wnt signaling. Remarkably, Ccd1 forms a hetero-complex with Dvl through the "head" of Dvl-DIX and the "tail" of Ccd1-DIX, depolymerizes Dvl homo-assembly, and thereby controls the size of Dvl polymer. These data together suggest a molecular mechanism for Ccd1-mediated Wnt activation in that Ccd1 converts latent polymeric Dvl to a biologically active oligomer(s).
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