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  An optochemical tool for light-induced dissociation of adherens junctions to control mechanical coupling between cells

Ollech, D., Pflästerer, Tim, T., Shellard, A., Zambarda, C., Spatz, J. P., Marcq, P., et al. (2020). An optochemical tool for light-induced dissociation of adherens junctions to control mechanical coupling between cells. Nature Communications, 11: 472 (2020), pp. 1-13. doi:10.1038/s41467-020-14390-1.

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 Creators:
Ollech, Dirk1, 2, 3, 4, Author           
Pflästerer, Tim, Tim, Author
Shellard, Adam, Author
Zambarda, Chiara1, 5, 6, Author           
Spatz, Joachim P.1, 7, Author           
Marcq, Philippe, Author
Mayor, Roberto, Author
Wombacher, Richard, Author
Cavalcanti-Adam, Elisabetta Ada1, 7, Author           
Affiliations:
1Cellular Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_2364731              
2Department of Biomedical Optics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497699              
3Light Microscopy Facility, Max Planck Institute for Medical Research, Max Planck Society, ou_1497720              
4Structure of neocortical circuits, Max Planck Institute for Medical Research, Max Planck Society, ou_1497742              
5Biophysical Chemistry, Institute of Physicla Chemistry, University of Heidelberg, 69120 Heidelberg, Germany, ou_persistent22              
6Dept. New Materials and Biosystems, Max Planck Institute for Intelligent Systems, Max Planck Society, ou_1497649              
7Biophysical Chemistry, Institute of Physical Chemistry, University of Heidelberg, 69120 Heidelberg, Germany, ou_persistent22              

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 Abstract: 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.

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Language(s): eng - English
 Dates: 2019-02-192020-01-072020-01-24
 Publication Status: Published online
 Pages: 13
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1038/s41467-020-14390-1
 Degree: -

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Title: Nature Communications
  Abbreviation : Nat. Commun.
Source Genre: Journal
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Publ. Info: London : Nature Publishing Group
Pages: - Volume / Issue: 11 Sequence Number: 472 (2020) Start / End Page: 1 - 13 Identifier: ISSN: 2041-1723
CoNE: https://pure.mpg.de/cone/journals/resource/2041-1723