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Crystal structure of a β-catenin/Axin complex suggests a mechanism for the β-catenin destruction complex
Open accessAbstract
The “β-catenin destruction complex” is central to canonical Wnt/β-catenin signaling. The scaffolding protein Axin and the tumor suppressor adenomatous polyposis coli protein (APC) are critical components of this complex, required for rapid β-catenin turnover. We determined the crystal structure of a complex between β-catenin and the β-catenin-binding domain of Axin (Axin-CBD). The Axin-CBD forms a helix that occupies the groove formed by the third and fourth armadillo repeats of β-catenin and thus precludes the simultaneous binding of other β-catenin partners in this region. Our biochemical studies demonstrate that, when phosphorylated, the 20-amino acid repeat region of APC competes with Axin for binding to β-catenin. We propose that a key function of APC in the β-catenin destruction complex is to remove phosphorylated β-catenin product from the active site.
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Wnt Signaling Modulates Routes of Retinoic Acid-Induced Differentiation of Embryonic Stem Cells
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“2004) and axin (Spink et al. 2000; Xing et al. 2003), targeting it toward degradation.”
BackgroundStructure-based engineering of the midnolin-proteasome pathway for targeted protein degradation
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Self-citationDexamethasone Modulates the Dynamics of Wnt Signaling in Human Trabecular Meshwork Cells
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“Axin also plays an important role in bringing β-catenin and GSK-3β together so that the phosphorylation and subsequent β-catenin can occur in states where there is no Wnt agonist available [48].”
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“Structural analysis suggests this motif is critical for Axin/β-catenin interactions, and this is confirmed by immunoprecipitation of mutant peptides (Xing et al., 2003).”
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“These three major transduction pathways are the Wnt/β-catenin classical pathway, the c-Jun NH2-terminal kinases (JNK) gene-mediated and participating planar cell polarity (PCP) pathway, and the Ca-mediated Wnt/Ca2+ pathways (Xing et al., 2003).”
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“[54].”
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“of this groove interact with several b-catenin ligands, including cadherins, Tcfs, APC, and Axin (Graham et al. 2000, 2001; von Kries et al. 2000; Huber and Weis 2001; Poy et al. 2001; Spink et al. 2001; Daniels and Weis 2002; Graham et al. 2002; Xing et al. 2002 ) (Fig. 2b and below).”
BackgroundNuclear β-catenin: molecular regulation, challenges and therapeutic opportunities
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“Key β-catenin binding partners, including TCF4 [114], TCF3 [114], LEF1 [115], AXIN2 [116], APC [117], BCL9 [118], ICAT (inhibitor of β-catenin and TCF-4) (See figure on previous page.)”
Metadata
- Authors
- Xing, Y., Clements, W. K., Kimelman, D., & Xu, W.
- Affiliations
- University of Washington (US)
- Venue
- Genes & Development
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2003-01-01
- Volume
- 17
- Issue
- 22
- Pages
- 2753-2764
- ISSN
- 0890-9369 (ISSN-L)
- 1549-5477
- PMC
- PMC280624
- OpenAlex
- W2041827225
- Semantic Scholar
- f02d1678de9728664b949b5fed44792fbdcc704e
- Cited by
- 237
- References
- 50
- Citations by year
- 2026: 7 · 2025: 6 · 2024: 10 · 2023: 9 · 2022: 15 · 2021: 9 · 2020: 10 · 2019: 11 · 2018: 7 · 2017: 10 · 2016: 7 · 2015: 9 · 2014: 16 · 2013: 12 · 2012: 14
- Type
- posted content
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Genes & Development (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- National Cancer Institute (CA 90351, R01CA090351)
- Eunice Kennedy Shriver National Institute of Child Health and Human Development (R01HD027262, HD27262)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Wnt/β-catenin signaling in development and cancer
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Signaling Pathways in Disease
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Keywords
- β-catenin, Axin, β-catenin destruction complex, Wnt/β-catenin signaling, adenomatous polyposis coli, armadillo repeats, protein-protein complex structure, β-catenin phosphorylation, protein turnover, tumor suppressor
- MeSH terms
- Amino Acid Sequence, Animals, Binding Sites, Cytoskeletal Proteins, Humans, Models, Molecular, Molecular Sequence Data, Phosphorylation, Protein Binding, Protein Conformation, Proteins, Repressor Proteins, Xenopus laevis, Signal Transduction, Trans-Activators, Sequence Homology, Amino Acid, Crystallography, X-Ray, Adenomatous Polyposis Coli Protein, Xenopus Proteins, beta Catenin, Axin Protein
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