ArticleDevelopmental biology2008
Unexpectedly robust assembly of the Axin destruction complex regulates Wnt/Wg signaling in Drosophila as revealed by analysis in vivo.
Article in Developmental biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers, 1 of them a synthesis that pooled it.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
42 citing papers in PubMed, 1 synthesis or guideline pooled it, 55 citations in OpenAlex.
- How short peptides interact with oral cells? A systematic review.BMC oral health · 2025Pooled it
- Reconstructing the evolutionary origin of β-catenin recognition in the Wnt destruction complex.Molecular biology and evolution · 2026Article
- Mechanistic insights into Wnt-β-catenin pathway activation and signal transduction.Nature reviews. Molecular cell biology · 2025Review
- Slit2/Robo1 signaling inhibits small-cell lung cancer by targeting β-catenin signaling in tumor cells and macrophages.Molecular oncology · 2023Article
- The Flavonol Quercitrin Hinders GSK3 Activity and Potentiates the Wnt/β-Catenin Signaling Pathway.International journal of molecular sciences · 2022Article
- An early global role for Axin is required for correct patterning of the anterior-posterior axis in the sea urchin embryo.Development (Cambridge, England) · 2021Article
- Lithium and Therapeutic Targeting of GSK-3.Cells · 2021Review
- Zooming in on the WNT/CTNNB1 Destruction Complex: Functional Mechanistic Details with Implications for Therapeutic Targeting.Handbook of experimental pharmacology · 2021Article
- The Scaffold Protein Axin Promotes Signaling Specificity within the Wnt Pathway by Suppressing Competing Kinase Reactions.Cell systems · 2020Article
- Limited dishevelled/Axin oligomerization determines efficiency of Wnt/β-catenin signal transduction.eLife · 2020Article
- Carboxy-Terminal Cementum Protein 1-Derived Peptide 4 (cemp1-p4) Promotes Mineralization through wnt/International journal of molecular sciences · 2020Article
- Destruction complex dynamics: Wnt/β-catenin signaling alters Axin-GSK3β interactionsDevelopment (Cambridge, England) · 2019Article
- A Context-Dependent Role for the RNF146 Ubiquitin Ligase in Wingless/Wnt Signaling inGenetics · 2019Article
- Wnt/Beta-Catenin Signaling Regulation and a Role for Biomolecular Condensates.Developmental cell · 2019Review
- Supramolecular assembly of the beta-catenin destruction complex and the effect of Wnt signaling on its localization, molecular size, and activity in vivo.PLoS genetics · 2018Article
- Molecular regulation and pharmacological targeting of the β-catenin destruction complex.British journal of pharmacology · 2017Review
- Regulation of Wnt/β-catenin signalling by tankyrase-dependent poly(ADP-ribosyl)ation and scaffolding.British journal of pharmacology · 2017Review
- Reconstituting regulation of the canonical Wnt pathway by engineering a minimal β-catenin destruction machine.Molecular biology of the cell · 2017Article
- Calcitonin gene-related peptide promotes the expression of osteoblastic genes and activates the WNT signal transduction pathway in bone marrow stromal stem cells.Molecular medicine reports · 2016Article
- The ADP-ribose polymerase Tankyrase regulates adult intestinal stem cell proliferation during homeostasis in Drosophila.Development (Cambridge, England) · 2016Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Secreted proteins in the Wnt family regulate gene expression in target cells by causing the accumulation of the transcriptional activator beta-catenin. In the absence of Wnt, a protein complex assembled around the scaffold protein Axin targets beta-catenin for destruction, thereby preventing it from transducing inappropriate signals. Loss of Axin or its binding partners APC and GSK3 results in aberrant activation of the Wnt signaling response. We have analyzed the effects of mutant forms of Drosophila Axin with large internal deletions when expressed at physiological levels in vivo, either in the presence or absence of wild type Axin. Surprisingly, even deletions that completely remove the binding sites for fly APC, GSK3 or beta-catenin, though they fail to rescue to viability, these mutant forms of Axin cause only mild developmental defects, indicating largely retained Axin function. Furthermore, two lethal Axin deletion constructs, AxinDeltaRGS and AxinDeltabeta cat(DeltaArm), can complement each other and restore viability. Our findings support a model in which the Axin complex is assembled through cooperative tripartite interactions among the binding partners, making the assembly of functional complexes surprisingly robust.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.