Distinct β-catenins mediate adhesion and signalling functions in C. elegans
Abstract
In flies and vertebrates, Armadillo/beta-catenin forms a complex with Tcf/Lef-1 transcription factors, serving as an essential co-activator to mediate Wnt signalling. It also associates with cadherins to mediate adhesion. In Caenorhabditis elegans, three putative beta-catenin homologues have been identified: WRM-1, BAR-1 and HMP-2. WRM-1 and the Tcf homologue POP-1 mediate Wnt signalling by a mechanism that has challenged current views of the Wnt pathway. Here we show that BAR-1 is the only beta-catenin homologue that interacts directly with POP-1. BAR-1 mediates Wnt signalling by forming a BAR-1/POP-1 bipartite transcription factor that activates expression of Wnt target genes such as the Hox gene mab-5. HMP-2 is the only beta-catenin homologue that interacts with the single cadherin of C. elegans, HMR-1. We conclude that a canonical Wnt pathway exists in C. elegans. Furthermore, our analysis shows that the functions of C. elegans beta-catenins in adhesion and in signalling are performed by separate proteins.
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POP-1 positively mediates Wnt signal in C. elegans.
“Korswagen et al. reported that POP-1 positively mediates Wnt signal in C. elegans.24)”
From Mammalian Nemo-like kinase enhances .BETA.-catenin-TCF transcription activity in human osteosarcoma and neuroblastoma cells (2007) · cites this paper as [24]
WRM-1 weakly binds full-length POP-1.
“Indeed, WRM-1, which is only 19% identical to vertebrate β-catenin, does not bind to the POP-1 β-catenin-binding domain per se but weakly binds full-length POP-1 (14, 19, 22).”
WRM-1 does not bind to the POP-1 β-catenin-binding domain per se.
“Indeed, WRM-1, which is only 19% identical to vertebrate β-catenin, does not bind to the POP-1 β-catenin-binding domain per se but weakly binds full-length POP-1 (14, 19, 22).”
WRM-1 is only 19% identical to vertebrate β-catenin.
“Indeed, WRM-1, which is only 19% identical to vertebrate β-catenin, does not bind to the POP-1 β-catenin-binding domain per se but weakly binds full-length POP-1 (14, 19, 22).”
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References 30 · Cited by 218
- Authors
- Korswagen, H. C., Herman, M. A., & Clevers, H. C.
- Affiliations
- University Medical Center Utrecht (NL)
- Kansas State University (US)
- Corresponding author
- Korswagen, Hendrik C.
- Venue
- Nature
- Published
- 2000-08-01
- Volume
- 406
- Issue
- 6795
- Pages
- 527-532
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W1858233634
- Cited by
- 218
- References
- 30
- Citations by year
- 2026: 3 · 2025: 4 · 2024: 1 · 2022: 5 · 2021: 2 · 2020: 3 · 2019: 4 · 2018: 7 · 2017: 7 · 2016: 5 · 2015: 18 · 2014: 17 · 2013: 8 · 2012: 11
- FWCI
- 4.70
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- Funders
- Nederlandse Organisatie voor Wetenschappelijk Onderzoek
- National Institutes of Health
- 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 › Developmental Biology and Gene Regulation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Hippo pathway signaling and YAP/TAZ
- Keywords
- β-catenin, POP-1, Wnt signaling, cell adhesion, cadherins, Hox genes, Caenorhabditis elegans, canonical Wnt pathway
- MeSH terms
- Animals, Cell Adhesion, Cell Line, Cloning, Molecular, Cytoskeletal Proteins, DNA-Binding Proteins, Gene Expression Regulation, High Mobility Group Proteins, Molecular Sequence Data, Mutation, Proto-Oncogene Proteins, Transcription Factors, Signal Transduction, Trans-Activators, Helminth Proteins, Caenorhabditis elegans, Genes, Helminth, Genes, Reporter, Homeodomain Proteins, Two-Hybrid System Techniques, Caenorhabditis elegans Proteins, Zebrafish Proteins, Animals, Genetically Modified, Wnt Proteins, beta Catenin, Mice
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