The Divergent Caenorhabditis elegans β-Catenin Proteins BAR-1, WRM-1 and HMP-2 Make Distinct Protein Interactions but Retain Functional Redundancy in Vivo
Abstract
β-Catenins function both in cell adhesion as part of the cadherin/catenin complex and in Wnt signal transduction as transcription factors. Vertebrates express two related proteins, β-catenin and plakoglobin, while Drosophila has a single family member, Armadillo. Caenorhabditis elegans expresses three β-catenin-related proteins, BAR-1, HMP-2, and WRM-1, which are quite diverged in sequence from each other and other β-catenins. While BAR-1 and WRM-1 are known to act in Wnt-mediated processes, and HMP-2 acts in a complex with cadherin/α-catenin homologs, it is unclear whether all three proteins retain the other functions of β-catenin. Here we show that BAR-1, like vertebrate β-catenin, has redundant transcription activation domains in its amino- and carboxyl-terminal regions but that HMP-2 and WRM-1 also possess the ability to activate transcription. We show via yeast two-hybrid analysis that these three proteins display distinct patterns of protein interactions. Surprisingly, we find that both WRM-1 and HMP-2 can substitute for BAR-1 in C. elegans when expressed from the bar-1 promoter. Therefore, although their mutant phenotypes and protein interaction patterns strongly suggest that the functions of β-catenin in other species have been segregated among three diverged proteins in C. elegans, these proteins still retain sufficient similarity to display functional redundancy in vivo.
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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).”
From Regulation of Lymphoid Enhancer Factor 1/T-Cell Factor by Mitogen-Activated Protein Kinase-Related Nemo-Like Kinase-Dependent Phosphorylation in Wnt/β-Catenin Signaling (2003) · cites this paper as [19]
The percentage-identity table in the section on β-catenin family members across species (page unavailable) gives 17% identity between WRM-1 and human β-catenin, not 19%. The Methods section says these percentages were calculated from sequence alignments. (LLM, conf=0.90)
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Experimental — accuracy not yet measuredWRM-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).”
From Regulation of Lymphoid Enhancer Factor 1/T-Cell Factor by Mitogen-Activated Protein Kinase-Related Nemo-Like Kinase-Dependent Phosphorylation in Wnt/β-Catenin Signaling (2003) · cites this paper as [19]
In the protein-interaction results (page unavailable), WRM-1 interacts weakly with POP-1 even after deletion of POP-1’s amino-terminal β-catenin-binding region. This supports an interaction that does not require that region, but the paper does not test whether WRM-1 can bind the region itself; it presents a different mode of interaction as a suggestion, not a categorical finding. (LLM, conf=0.84)
Experimental — accuracy not yet measuredWRM-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).”
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Cites
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Ishitani, T., Ninomiya-Tsuji, J., & Matsumoto, K. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.4.1379-1389.2003 · Cited by 212 · see citing works
Adamska, M., Larroux, C., Adamski, M., Green, K., Lovas, E., Koop, D., Richards, G. S., Zwafink, C., & Degnan, B. M. (2010) · Evolution & Development · doi:10.1111/j.1525-142x.2010.00435.x · Cited by 139 · see citing works
- Authors
- Natarajan, L., Witwer, N. E., & Eisenmann, D. M.
- Affiliations
- University of Maryland, Baltimore County (US)
- Corresponding author
- Eisenmann, David M
- ORCID
- Eisenmann, David M
- Venue
- Genetics
- Publisher
- Oxford University Press (OUP)
- Published
- 2001-09-01
- Volume
- 159
- Issue
- 1
- Pages
- 159-172
- ISSN
- 0016-6731 (ISSN-L)
- 1943-2631
- OpenAlex
- W2171635426
- Cited by
- 75
- References
- 1
- Citations by year
- 2026: 1 · 2025: 1 · 2021: 1 · 2020: 2 · 2018: 2 · 2017: 4 · 2016: 1 · 2015: 1 · 2014: 5 · 2013: 3 · 2012: 6
- FWCI
- 1.63
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- academic.oup.com/journals/pages/open_access/funder_policies/chorus/standard_publication_model (vor)
- Locations
- Genetics (publishedVersion)
- PubMed (publishedVersion)
- 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 › Molecular Biology › Signaling Pathways in Disease
- Keywords
- β-catenin, Caenorhabditis elegans, functional redundancy, Wnt signaling, transactivation domain, protein-protein interaction, cadherin-catenin complex, cell adhesion, gene substitution
- MeSH terms
- Animals, Cell Adhesion, Cytoskeletal Proteins, Dose-Response Relationship, Drug, Models, Genetic, Oligonucleotides, Phenotype, Phylogeny, Protein Binding, Transcription Factors, Transcription, Genetic, Transcriptional Activation, Trans-Activators, Caenorhabditis elegans, Protein Structure, Tertiary, Databases as Topic, Two-Hybrid System Techniques, Caenorhabditis elegans Proteins, beta Catenin
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