E-cadherin is under constitutive actomyosin-generated tension that is increased at cell-cell contacts upon externally applied stretch. Borghi, N., Sorokina, M., Shcherbakova, O., Weis, W., Pruitt, B., Nelson, W., & Dunn, A. Proceedings of the National Academy of Sciences of the United States of America, 109(31):12568-12573, National Academy of Sciences, 2012. cited By 284
E-cadherin is under constitutive actomyosin-generated tension that is increased at cell-cell contacts upon externally applied stretch [link]Paper  doi  abstract   bibtex   
Classical cadherins are transmembrane proteins at the core of intercellular adhesion complexes in cohesive metazoan tissues. The extracellular domain of classical cadherins forms intercellular bonds with cadherins on neighboring cells, whereas the cytoplasmic domain recruits catenins, which in turn associate with additional cytoskeleton binding and regulatory proteins. Cadherin/catenin complexes are hypothesized to play a role in the transduction of mechanical forces that shape cells and tissues during development, regeneration, and disease. Whether mechanical forces are transduced directly through cadherins is unknown. To address this question, we used a Förster resonance energy transfer (FRET)-based molecular tension sensor to test the origin and magnitude of tensile forces transmitted through the cytoplasmic domain of E-cadherin in epithelial cells. We show that the actomyosin cytoskeleton exerts pN-tensile force on E-cadherin, and that this tension requires the catenin-binding domain of E-cadherin and αE-catenin. Surprisingly, the actomyosin cytoskeleton constitutively exerts tension on E-cadherin at the plasma membrane regardless of whether or not E-cadherin is recruited to cell-cell contacts, although tension is further increased at cell-cell contacts when adhering cells are stretched. Our findings thus point to a constitutive role of E-cadherin in transducing mechanical forces between the actomyosin cytoskeleton and the plasmamembrane, not only at cell-cell junctions but throughout the cell surface.
@ARTICLE{Borghi201212568,
author={Borghi, N. and Sorokina, M. and Shcherbakova, O.G. and Weis, W.I. and Pruitt, B.L. and Nelson, W.J. and Dunn, A.R.},
title={E-cadherin is under constitutive actomyosin-generated tension that is increased at cell-cell contacts upon externally applied stretch},
journal={Proceedings of the National Academy of Sciences of the United States of America},
year={2012},
volume={109},
number={31},
pages={12568-12573},
doi={10.1073/pnas.1204390109},
note={cited By 284},
url={https://www.scopus.com/inward/record.uri?eid=2-s2.0-84864506988&doi=10.1073%2fpnas.1204390109&partnerID=40&md5=27a25f91d046dadaaa32776ddecb5cfa},
affiliation={Department of Biology, Stanford University, Stanford, CA 94305, United States; Department of Mechanical Engineering, Stanford University, Stanford, CA 94305, United States; Department of Chemical Engineering, Stanford University, Stanford, CA 94305, United States; Department of Structural Biology, Stanford University, Stanford, CA 94305, United States; Department of Molecular and Cellular Physiology, Stanford University, Stanford, CA 94305, United States; Department of Cell Biology, Centre National de la Recherche Scientifique, Université Paris-Diderot, Paris 75013, France},
abstract={Classical cadherins are transmembrane proteins at the core of intercellular adhesion complexes in cohesive metazoan tissues. The extracellular domain of classical cadherins forms intercellular bonds with cadherins on neighboring cells, whereas the cytoplasmic domain recruits catenins, which in turn associate with additional cytoskeleton binding and regulatory proteins. Cadherin/catenin complexes are hypothesized to play a role in the transduction of mechanical forces that shape cells and tissues during development, regeneration, and disease. Whether mechanical forces are transduced directly through cadherins is unknown. To address this question, we used a Förster resonance energy transfer (FRET)-based molecular tension sensor to test the origin and magnitude of tensile forces transmitted through the cytoplasmic domain of E-cadherin in epithelial cells. We show that the actomyosin cytoskeleton exerts pN-tensile force on E-cadherin, and that this tension requires the catenin-binding domain of E-cadherin and αE-catenin. Surprisingly, the actomyosin cytoskeleton constitutively exerts tension on E-cadherin at the plasma membrane regardless of whether or not E-cadherin is recruited to cell-cell contacts, although tension is further increased at cell-cell contacts when adhering cells are stretched. Our findings thus point to a constitutive role of E-cadherin in transducing mechanical forces between the actomyosin cytoskeleton and the plasmamembrane, not only at cell-cell junctions but throughout the cell surface.},
author_keywords={Mechanobiology;  Mechanosensor;  Mechanotransduction;  Morphogenesis;  Signal transduction},
correspondence_address1={Dunn, A.R.; Department of Chemical Engineering, Stanford University, Stanford, CA 94305, United States; email: alex.dunn@stanford.edu},
publisher={National Academy of Sciences},
issn={00278424},
coden={PNASA},
pubmed_id={22802638},
language={English},
abbrev_source_title={Proc. Natl. Acad. Sci. U. S. A.},
document_type={Article},
source={Scopus},
}
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