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Catenins are characterized by multiple binding domains and dynamic structures that allow them to function as linker proteins in cell junction complexes. All catenins, except α-catenin, contain a characteristic protein sequence called the armadillo repeat and are therefore also called armadillo proteins.
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The gene encoding the main signaling molecules of the Wnt signaling pathways (the Wnt proteins) was discovered almost four decades ago by Nüsslein-Volhard and Wieschaus. They identified and originally named the gene "wingless" (wg) after a phenotype discovered during their landmark genetic screen in Drosophila for body pattern defects. At around the same time, another researcher named Harold Varmus found that a murine tumor virus activates the mammalian wg homolog, Int-1, which...
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Proteins targeted to the nucleus carry short stretches of amino acid sequences called the nuclear localization signal or NLS. Classical nuclear localization signals are of two types: monopartite and bipartite NLS. Monopartite classical NLS (cNLS) consists of a single cluster of 4-8 amino acids. Bipartite cNLS consists of two clusters of  2-3 amino acids and a 9-12 residue long proline-rich linker bridging the two clusters. Signal clusters are rich in positively charged amino acids such as...
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The nucleus restricts several proteins within and allows others to pass. The restricted proteins possess a nuclear retention sequence or NRS, anchoring them to the nuclear lamins and preventing their transport to the cytosol. The non-restricted proteins, after their synthesis, are transported to their site of action, such as the cytosol or other organelles, with the help of nuclear export signals or NES.
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Nuclear protein sorting is the selective trafficking of histones, polymerases, gene regulatory proteins into the nucleus and exporting RNAs and ribosomes to the cytosol. It is a tightly controlled process that regulates gene expression within a cell.
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Related Experiment Video

Updated: Apr 8, 2026

Reconstitution Of β-catenin Degradation In Xenopus Egg Extract
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Nuclear β-Catenin under Control.

François Fagotto1

  • 1Department of Biology, McGill University, Montreal H3A1B1, Quebec, Canada.

Developmental Cell
|June 24, 2015
PubMed
Summary
This summary is machine-generated.

This study reveals a novel mechanism for degrading nuclear beta-catenin (a key protein in Wnt signaling) by linking lysine demethylation to ubiquitination, controlling gene transcription.

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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • Beta-catenin (a key protein in Wnt signaling) accumulates in the nucleus during Wnt stimulation.
  • Nuclear beta-catenin regulates gene transcription, impacting various cellular processes.
  • Understanding the regulation of nuclear beta-catenin is crucial for deciphering Wnt pathway signaling.

Purpose of the Study:

  • To elucidate the mechanism targeting nuclear beta-catenin for degradation.
  • To identify the role of lysine demethylation in regulating nuclear beta-catenin stability.
  • To investigate how ubiquitination is signaled in the context of nuclear beta-catenin.

Main Methods:

  • Utilized biochemical assays to study protein interactions.
  • Employed molecular biology techniques to investigate ubiquitination and demethylation.
  • Analyzed the impact of specific modifications on beta-catenin stability and localization.

Main Results:

  • Identified a novel mechanism linking lysine demethylation to beta-catenin ubiquitination.
  • Demonstrated that lysine demethylation specifically targets the nuclear pool of beta-catenin for degradation.
  • Showcased a new layer of regulation for Wnt/beta-catenin signaling.

Conclusions:

  • Lysine demethylation serves as a signal for beta-catenin ubiquitination and subsequent degradation.
  • This mechanism provides specific control over the nuclear beta-catenin pool.
  • The findings offer new insights into the complex regulation of Wnt signaling.