Please use this identifier to cite or link to this item: https://doi.org/10.1371/journal.pbio.0020095
Title: A nuclear function for armadillo/?-catenin
Authors: Tolwinski N.S. 
Wieschaus E.
Keywords: catenin
Wnt protein
armadillo domain protein
armadillo protein, Drosophila
beta catenin
carrier protein
Chibby protein, Drosophila
Drosophila protein
nuclear protein
transcription factor
allele
article
controlled study
Drosophila
embryo
missense mutation
nonhuman
nucleotide sequence
point mutation
protein function
protein localization
protein stability
signal transduction
transcription initiation
animal
cell membrane
cell nucleus
cross breeding
Drosophila melanogaster
fluorescence microscopy
metabolism
molecular genetics
mutation
phenotype
physiology
protein tertiary structure
transgene
Western blotting
Armadillo
Invertebrata
Vertebrata
Alleles
Animals
Armadillo Domain Proteins
beta Catenin
Blotting, Western
Carrier Proteins
Cell Membrane
Cell Nucleus
Crosses, Genetic
Drosophila melanogaster
Drosophila Proteins
Microscopy, Fluorescence
Molecular Sequence Data
Mutation
Mutation, Missense
Nuclear Proteins
Phenotype
Protein Structure, Tertiary
Signal Transduction
Transcription Factors
Transgenes
Wnt Proteins
Issue Date: 2004
Citation: Tolwinski N.S., Wieschaus E. (2004). A nuclear function for armadillo/?-catenin. PLoS Biology 2 (4). ScholarBank@NUS Repository. https://doi.org/10.1371/journal.pbio.0020095
Abstract: The Wnt signaling pathway provides key information during development of vertebrates and invertebrates, and mutations in this pathway lead to various forms of cancer. Wnt binding to its receptor causes the stabilization and nuclear localization of ?-catenin. Nuclear ?-catenin then functions to activate transcription in conjunction with the transcription factor TCF. A recent report has challenged this basic precept of the Wnt signaling field, arguing that the nuclear localization of ?-catenin may be unrelated to its function and that ?-catenin functions at the plasma membrane to activate this signaling pathway. Here we present evidence that the pathway in fact does depend on the nuclear localization of ?-catenin. We reexamine the functionality of various truncations of ?-catenin and find that only the most severe truncations are true signaling-null mutations. Further, we define a signaling-null condition and use it to show that membrane-tethered ?-catenin is insufficient to activate transcription. We also define two novel loss-of-function mutations that are not truncations, but are missense point mutations that retain protein stability. These alleles allow us to show that the membrane-bound form of activated ?-catenin does indeed depend on the endogenous protein. Further, this activity is dependent on the presence of the C-terminus-specific negative regulator Chibby. Our data clearly show that nuclear localization of ?-catenin is in fact necessary for Wnt pathway activation.
Source Title: PLoS Biology
URI: https://scholarbank.nus.edu.sg/handle/10635/161692
ISSN: 15449173
DOI: 10.1371/journal.pbio.0020095
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