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Remodeling the zonula adherens in response to tension and the role of afadin in this response
Morphogenesis requires dynamic coordination between cell–cell adhesion and the cytoskeleton to allow cells to change shape and move without losing tissue integrity. We used genetic tools and superresolution microscopy in a simple model epithelial cell line to define how the molecular architecture of...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The Rockefeller University Press
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5084271/ https://www.ncbi.nlm.nih.gov/pubmed/27114502 http://dx.doi.org/10.1083/jcb.201506115 |
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author | Choi, Wangsun Acharya, Bipul R. Peyret, Grégoire Fardin, Marc-Antoine Mège, René-Marc Ladoux, Benoit Yap, Alpha S. Fanning, Alan S. Peifer, Mark |
author_facet | Choi, Wangsun Acharya, Bipul R. Peyret, Grégoire Fardin, Marc-Antoine Mège, René-Marc Ladoux, Benoit Yap, Alpha S. Fanning, Alan S. Peifer, Mark |
author_sort | Choi, Wangsun |
collection | PubMed |
description | Morphogenesis requires dynamic coordination between cell–cell adhesion and the cytoskeleton to allow cells to change shape and move without losing tissue integrity. We used genetic tools and superresolution microscopy in a simple model epithelial cell line to define how the molecular architecture of cell–cell zonula adherens (ZA) is modified in response to elevated contractility, and how these cells maintain tissue integrity. We previously found that depleting zonula occludens 1 (ZO-1) family proteins in MDCK cells induces a highly organized contractile actomyosin array at the ZA. We find that ZO knockdown elevates contractility via a Shroom3/Rho-associated, coiled-coil containing protein kinase (ROCK) pathway. Our data suggest that each bicellular border is an independent contractile unit, with actin cables anchored end-on to cadherin complexes at tricellular junctions. Cells respond to elevated contractility by increasing junctional afadin. Although ZO/afadin knockdown did not prevent contractile array assembly, it dramatically altered cell shape and barrier function in response to elevated contractility. We propose that afadin acts as a robust protein scaffold that maintains ZA architecture at tricellular junctions. |
format | Online Article Text |
id | pubmed-5084271 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-50842712016-10-31 Remodeling the zonula adherens in response to tension and the role of afadin in this response Choi, Wangsun Acharya, Bipul R. Peyret, Grégoire Fardin, Marc-Antoine Mège, René-Marc Ladoux, Benoit Yap, Alpha S. Fanning, Alan S. Peifer, Mark J Cell Biol Research Articles Morphogenesis requires dynamic coordination between cell–cell adhesion and the cytoskeleton to allow cells to change shape and move without losing tissue integrity. We used genetic tools and superresolution microscopy in a simple model epithelial cell line to define how the molecular architecture of cell–cell zonula adherens (ZA) is modified in response to elevated contractility, and how these cells maintain tissue integrity. We previously found that depleting zonula occludens 1 (ZO-1) family proteins in MDCK cells induces a highly organized contractile actomyosin array at the ZA. We find that ZO knockdown elevates contractility via a Shroom3/Rho-associated, coiled-coil containing protein kinase (ROCK) pathway. Our data suggest that each bicellular border is an independent contractile unit, with actin cables anchored end-on to cadherin complexes at tricellular junctions. Cells respond to elevated contractility by increasing junctional afadin. Although ZO/afadin knockdown did not prevent contractile array assembly, it dramatically altered cell shape and barrier function in response to elevated contractility. We propose that afadin acts as a robust protein scaffold that maintains ZA architecture at tricellular junctions. The Rockefeller University Press 2016-04-25 /pmc/articles/PMC5084271/ /pubmed/27114502 http://dx.doi.org/10.1083/jcb.201506115 Text en © 2016 Choi 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.rupress.org/terms). 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 Choi, Wangsun Acharya, Bipul R. Peyret, Grégoire Fardin, Marc-Antoine Mège, René-Marc Ladoux, Benoit Yap, Alpha S. Fanning, Alan S. Peifer, Mark Remodeling the zonula adherens in response to tension and the role of afadin in this response |
title | Remodeling the zonula adherens in response to tension and the role of afadin in this response |
title_full | Remodeling the zonula adherens in response to tension and the role of afadin in this response |
title_fullStr | Remodeling the zonula adherens in response to tension and the role of afadin in this response |
title_full_unstemmed | Remodeling the zonula adherens in response to tension and the role of afadin in this response |
title_short | Remodeling the zonula adherens in response to tension and the role of afadin in this response |
title_sort | remodeling the zonula adherens in response to tension and the role of afadin in this response |
topic | Research Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5084271/ https://www.ncbi.nlm.nih.gov/pubmed/27114502 http://dx.doi.org/10.1083/jcb.201506115 |
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