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Activity of the β-catenin phosphodestruction complex at cell–cell contacts is enhanced by cadherin-based adhesion
It is well established that cadherin protein levels impact canonical Wnt signaling through binding and sequestering β-catenin (β-cat) from T-cell factor family transcription factors. Whether changes in intercellular adhesion can affect β-cat signaling and the mechanism through which this occurs has...
Autores principales: | , , , , |
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Formato: | Texto |
Lenguaje: | English |
Publicado: |
The Rockefeller University Press
2009
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2717642/ https://www.ncbi.nlm.nih.gov/pubmed/19620634 http://dx.doi.org/10.1083/jcb.200811108 |
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author | Maher, Meghan T. Flozak, Annette S. Stocker, Adam M. Chenn, Anjen Gottardi, Cara J. |
author_facet | Maher, Meghan T. Flozak, Annette S. Stocker, Adam M. Chenn, Anjen Gottardi, Cara J. |
author_sort | Maher, Meghan T. |
collection | PubMed |
description | It is well established that cadherin protein levels impact canonical Wnt signaling through binding and sequestering β-catenin (β-cat) from T-cell factor family transcription factors. Whether changes in intercellular adhesion can affect β-cat signaling and the mechanism through which this occurs has remained unresolved. We show that axin, APC2, GSK-3β and N-terminally phosphorylated forms of β-cat can localize to cell–cell contacts in a complex that is molecularly distinct from the cadherin–catenin adhesive complex. Nonetheless, cadherins can promote the N-terminal phosphorylation of β-cat, and cell–cell adhesion increases the turnover of cytosolic β-cat. Together, these data suggest that cadherin-based cell–cell adhesion limits Wnt signals by promoting the activity of a junction-localized β-cat phosphodestruction complex, which may be relevant to tissue morphogenesis and cell fate decisions during development. |
format | Text |
id | pubmed-2717642 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2009 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-27176422010-01-27 Activity of the β-catenin phosphodestruction complex at cell–cell contacts is enhanced by cadherin-based adhesion Maher, Meghan T. Flozak, Annette S. Stocker, Adam M. Chenn, Anjen Gottardi, Cara J. J Cell Biol Research Articles It is well established that cadherin protein levels impact canonical Wnt signaling through binding and sequestering β-catenin (β-cat) from T-cell factor family transcription factors. Whether changes in intercellular adhesion can affect β-cat signaling and the mechanism through which this occurs has remained unresolved. We show that axin, APC2, GSK-3β and N-terminally phosphorylated forms of β-cat can localize to cell–cell contacts in a complex that is molecularly distinct from the cadherin–catenin adhesive complex. Nonetheless, cadherins can promote the N-terminal phosphorylation of β-cat, and cell–cell adhesion increases the turnover of cytosolic β-cat. Together, these data suggest that cadherin-based cell–cell adhesion limits Wnt signals by promoting the activity of a junction-localized β-cat phosphodestruction complex, which may be relevant to tissue morphogenesis and cell fate decisions during development. The Rockefeller University Press 2009-07-27 /pmc/articles/PMC2717642/ /pubmed/19620634 http://dx.doi.org/10.1083/jcb.200811108 Text en © 2009 Maher et al. This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.jcb.org/misc/terms.shtml). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/). |
spellingShingle | Research Articles Maher, Meghan T. Flozak, Annette S. Stocker, Adam M. Chenn, Anjen Gottardi, Cara J. Activity of the β-catenin phosphodestruction complex at cell–cell contacts is enhanced by cadherin-based adhesion |
title | Activity of the β-catenin phosphodestruction complex at cell–cell contacts is enhanced by cadherin-based adhesion |
title_full | Activity of the β-catenin phosphodestruction complex at cell–cell contacts is enhanced by cadherin-based adhesion |
title_fullStr | Activity of the β-catenin phosphodestruction complex at cell–cell contacts is enhanced by cadherin-based adhesion |
title_full_unstemmed | Activity of the β-catenin phosphodestruction complex at cell–cell contacts is enhanced by cadherin-based adhesion |
title_short | Activity of the β-catenin phosphodestruction complex at cell–cell contacts is enhanced by cadherin-based adhesion |
title_sort | activity of the β-catenin phosphodestruction complex at cell–cell contacts is enhanced by cadherin-based adhesion |
topic | Research Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2717642/ https://www.ncbi.nlm.nih.gov/pubmed/19620634 http://dx.doi.org/10.1083/jcb.200811108 |
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