Evidence map›Paper›PMID 11560894›Full record

ArticleGenetics2001

The divergent Caenorhabditis elegans beta-catenin proteins BAR-1, WRM-1 and HMP-2 make distinct protein interactions but retain functional redundancy in vivo.

L Natarajan, N E Witwer, D M Eisenmann

Open access · bronzeAbstract read
In one paragraph

Article in Genetics, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
1.6field-weighted citation impact, top 17% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

32 citing papers in PubMed, 75 citations in OpenAlex.

  1. Article
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  3. Review
  4. Article
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  6. Review
  7. β-Catenin-related protein WRM-1 is a multifunctional regulatory subunit of the LIT-1 MAPK complex.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Cadherins and their partners in the nematode worm Caenorhabditis elegans.Progress in molecular biology and translational science · 2013
    Review
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Repression of Wnt signaling by a Fer-type nonreceptor tyrosine kinase.Proceedings of the National Academy of Sciences of the United States of America · 2010
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

L NatarajanDepartment of Biological Sciences, University of Maryland, Baltimore County, Baltimore, Maryland 21250.
N E Witwer
D M Eisenmann
University of Maryland, Baltimore County · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

beta-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, beta-catenin and plakoglobin, while Drosophila has a single family member, Armadillo. Caenorhabditis elegans expresses three beta-catenin-related proteins, BAR-1, HMP-2, and WRM-1, which are quite diverged in sequence from each other and other beta-catenins. While BAR-1 and WRM-1 are known to act in Wnt-mediated processes, and HMP-2 acts in a complex with cadherin/alpha-catenin homologs, it is unclear whether all three proteins retain the other functions of beta-catenin. Here we show that BAR-1, like vertebrate beta-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 beta-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.

Indexed as

Caenorhabditis elegans ProteinsTrans-ActivatorsAnimalsbeta CateninCaenorhabditis elegansCell AdhesionCytoskeletal ProteinsDatabases as TopicDose-Response Relationship, DrugModels, GeneticOligonucleotidesPhenotypePhylogenyProtein BindingProtein Structure, TertiaryTranscriptional Activationbar-1 protein, C elegansbeta CateninCaenorhabditis elegans ProteinsCytoskeletal ProteinsHMP-2 protein, C elegansOligonucleotidesTrans-ActivatorsTranscription FactorsWRM-1 protein, C elegans

Identifiers

PMID11560894
PMCPMC1461775
OpenAlexW2171635426

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

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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.