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

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Ollech,  Dirk
Cellular Biophysics, Max Planck Institute for Medical Research, Max Planck Society;
Department of Biomedical Optics, Max Planck Institute for Medical Research, Max Planck Society;
Light Microscopy Facility, Max Planck Institute for Medical Research, Max Planck Society;
Structure of neocortical circuits, Max Planck Institute for Medical Research, Max Planck Society;

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Zambarda,  Chiara
Cellular Biophysics, Max Planck Institute for Medical Research, Max Planck Society;
Biophysical Chemistry, Institute of Physicla Chemistry, University of Heidelberg, 69120 Heidelberg, Germany;
Dept. New Materials and Biosystems, Max Planck Institute for Intelligent Systems, Max Planck Society;

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Spatz,  Joachim P.
Cellular Biophysics, Max Planck Institute for Medical Research, Max Planck Society;
Biophysical Chemistry, Institute of Physical Chemistry, University of Heidelberg, 69120 Heidelberg, Germany;

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Cavalcanti-Adam,  Elisabetta Ada
Cellular Biophysics, Max Planck Institute for Medical Research, Max Planck Society;
Biophysical Chemistry, Institute of Physical Chemistry, University of Heidelberg, 69120 Heidelberg, Germany;

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Citation

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.


Cite as: https://hdl.handle.net/21.11116/0000-0005-903C-5
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.