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An optochemical tool for light-induced dissociation of adherens junctions to control mechanical coupling between cells
The cadherin-catenin complex at adherens junctions (AJs) is essential for the formation of cell-cell adhesion and epithelium integrity; however, studying the dynamic regulation of AJs at high spatio-temporal resolution remains challenging. Here we present an optochemical tool which allows reconstitu...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6981158/ https://www.ncbi.nlm.nih.gov/pubmed/31980653 http://dx.doi.org/10.1038/s41467-020-14390-1 |
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author | Ollech, Dirk Pflästerer, Tim Shellard, Adam Zambarda, Chiara Spatz, Joachim Pius Marcq, Philippe Mayor, Roberto Wombacher, Richard Cavalcanti-Adam, Elisabetta Ada |
author_facet | Ollech, Dirk Pflästerer, Tim Shellard, Adam Zambarda, Chiara Spatz, Joachim Pius Marcq, Philippe Mayor, Roberto Wombacher, Richard Cavalcanti-Adam, Elisabetta Ada |
author_sort | Ollech, Dirk |
collection | PubMed |
description | The cadherin-catenin complex at adherens junctions (AJs) is essential for the formation of cell-cell adhesion and epithelium integrity; however, studying the dynamic regulation of AJs at high spatio-temporal resolution remains challenging. Here we present an optochemical tool which allows reconstitution of AJs by chemical dimerization of the force bearing structures and their precise light-induced dissociation. For the dimerization, we reconstitute acto-myosin connection of a tailless E-cadherin by two ways: direct recruitment of α-catenin, and linking its cytosolic tail to the transmembrane domain. Our approach enables a specific ON-OFF switch for mechanical coupling between cells that can be controlled spatially on subcellular or tissue scale via photocleavage. The combination with cell migration analysis and traction force microscopy shows a wide-range of applicability and confirms the mechanical contribution of the reconstituted AJs. Remarkably, in vivo our tool is able to control structural and functional integrity of the epidermal layer in developing Xenopus embryos. |
format | Online Article Text |
id | pubmed-6981158 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-69811582020-01-27 An optochemical tool for light-induced dissociation of adherens junctions to control mechanical coupling between cells Ollech, Dirk Pflästerer, Tim Shellard, Adam Zambarda, Chiara Spatz, Joachim Pius Marcq, Philippe Mayor, Roberto Wombacher, Richard Cavalcanti-Adam, Elisabetta Ada Nat Commun Article The cadherin-catenin complex at adherens junctions (AJs) is essential for the formation of cell-cell adhesion and epithelium integrity; however, studying the dynamic regulation of AJs at high spatio-temporal resolution remains challenging. Here we present an optochemical tool which allows reconstitution of AJs by chemical dimerization of the force bearing structures and their precise light-induced dissociation. For the dimerization, we reconstitute acto-myosin connection of a tailless E-cadherin by two ways: direct recruitment of α-catenin, and linking its cytosolic tail to the transmembrane domain. Our approach enables a specific ON-OFF switch for mechanical coupling between cells that can be controlled spatially on subcellular or tissue scale via photocleavage. The combination with cell migration analysis and traction force microscopy shows a wide-range of applicability and confirms the mechanical contribution of the reconstituted AJs. Remarkably, in vivo our tool is able to control structural and functional integrity of the epidermal layer in developing Xenopus embryos. Nature Publishing Group UK 2020-01-24 /pmc/articles/PMC6981158/ /pubmed/31980653 http://dx.doi.org/10.1038/s41467-020-14390-1 Text en © The Author(s) 2020 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article Ollech, Dirk Pflästerer, Tim Shellard, Adam Zambarda, Chiara Spatz, Joachim Pius Marcq, Philippe Mayor, Roberto Wombacher, Richard Cavalcanti-Adam, Elisabetta Ada An optochemical tool for light-induced dissociation of adherens junctions to control mechanical coupling between cells |
title | An optochemical tool for light-induced dissociation of adherens junctions to control mechanical coupling between cells |
title_full | An optochemical tool for light-induced dissociation of adherens junctions to control mechanical coupling between cells |
title_fullStr | An optochemical tool for light-induced dissociation of adherens junctions to control mechanical coupling between cells |
title_full_unstemmed | An optochemical tool for light-induced dissociation of adherens junctions to control mechanical coupling between cells |
title_short | An optochemical tool for light-induced dissociation of adherens junctions to control mechanical coupling between cells |
title_sort | optochemical tool for light-induced dissociation of adherens junctions to control mechanical coupling between cells |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6981158/ https://www.ncbi.nlm.nih.gov/pubmed/31980653 http://dx.doi.org/10.1038/s41467-020-14390-1 |
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