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The nonredundant nature of the Axin2 regulatory network in the canonical Wnt signaling pathway
Axin is one of two essential scaffolds in the canonical Wnt pathway that converts signals at the plasma membrane to signals inhibiting the degradation of β-catenin, leading to its accumulation and specific gene activation. In vertebrates, there are two forms of Axin, Axin1 and Axin2, which are simil...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
National Academy of Sciences
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8892335/ https://www.ncbi.nlm.nih.gov/pubmed/35197279 http://dx.doi.org/10.1073/pnas.2108408119 |
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author | Moshkovsky, Ana R. Kirschner, Marc W. |
author_facet | Moshkovsky, Ana R. Kirschner, Marc W. |
author_sort | Moshkovsky, Ana R. |
collection | PubMed |
description | Axin is one of two essential scaffolds in the canonical Wnt pathway that converts signals at the plasma membrane to signals inhibiting the degradation of β-catenin, leading to its accumulation and specific gene activation. In vertebrates, there are two forms of Axin, Axin1 and Axin2, which are similar at the protein level and genetically redundant. We show here that differential regulation of the two genes on the transcriptional and proteostatic level confers differential responsiveness that can be used in tissue-specific regulation. Such subtle features may distinguish other redundant gene pairs that are commonly found in vertebrates through gene knockout experiments. |
format | Online Article Text |
id | pubmed-8892335 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | National Academy of Sciences |
record_format | MEDLINE/PubMed |
spelling | pubmed-88923352022-08-23 The nonredundant nature of the Axin2 regulatory network in the canonical Wnt signaling pathway Moshkovsky, Ana R. Kirschner, Marc W. Proc Natl Acad Sci U S A Biological Sciences Axin is one of two essential scaffolds in the canonical Wnt pathway that converts signals at the plasma membrane to signals inhibiting the degradation of β-catenin, leading to its accumulation and specific gene activation. In vertebrates, there are two forms of Axin, Axin1 and Axin2, which are similar at the protein level and genetically redundant. We show here that differential regulation of the two genes on the transcriptional and proteostatic level confers differential responsiveness that can be used in tissue-specific regulation. Such subtle features may distinguish other redundant gene pairs that are commonly found in vertebrates through gene knockout experiments. National Academy of Sciences 2022-02-23 2022-03-01 /pmc/articles/PMC8892335/ /pubmed/35197279 http://dx.doi.org/10.1073/pnas.2108408119 Text en Copyright © 2022 the Author(s). Published by PNAS. https://creativecommons.org/licenses/by-nc-nd/4.0/This article is distributed under Creative Commons Attribution-NonCommercial-NoDerivatives License 4.0 (CC BY-NC-ND) (https://creativecommons.org/licenses/by-nc-nd/4.0/) . |
spellingShingle | Biological Sciences Moshkovsky, Ana R. Kirschner, Marc W. The nonredundant nature of the Axin2 regulatory network in the canonical Wnt signaling pathway |
title | The nonredundant nature of the Axin2 regulatory network in the canonical Wnt signaling pathway |
title_full | The nonredundant nature of the Axin2 regulatory network in the canonical Wnt signaling pathway |
title_fullStr | The nonredundant nature of the Axin2 regulatory network in the canonical Wnt signaling pathway |
title_full_unstemmed | The nonredundant nature of the Axin2 regulatory network in the canonical Wnt signaling pathway |
title_short | The nonredundant nature of the Axin2 regulatory network in the canonical Wnt signaling pathway |
title_sort | nonredundant nature of the axin2 regulatory network in the canonical wnt signaling pathway |
topic | Biological Sciences |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8892335/ https://www.ncbi.nlm.nih.gov/pubmed/35197279 http://dx.doi.org/10.1073/pnas.2108408119 |
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