Please use this identifier to cite or link to this item: https://doi.org/10.1126/sciadv.aav2720
Title: Direct single-molecule quantification reveals unexpectedly high mechanical stability of vinculin—talin/?-catenin linkages
Authors: Le, S. 
Yu, M. 
Yan, J. 
Issue Date: 2019
Publisher: American Association for the Advancement of Science
Citation: Le, S., Yu, M., Yan, J. (2019). Direct single-molecule quantification reveals unexpectedly high mechanical stability of vinculin—talin/?-catenin linkages. Science Advances 5 (12) : eaav2720. ScholarBank@NUS Repository. https://doi.org/10.1126/sciadv.aav2720
Rights: Attribution-NonCommercial 4.0 International
Abstract: The vinculin-mediated mechanosensing requires establishment of stable mechanical linkages between vinculin to integrin at focal adhesions and to cadherins at adherens junctions through associations with the respective adaptor proteins talin and ?-catenin. However, the mechanical stability of these critical vinculin linkages has yet to be determined. Here, we developed a single-molecule detector assay to provide direct quantification of the mechanical lifetime of vinculin association with the vinculin binding sites in both talin and ?-catenin, which reveals a surprisingly high mechanical stability of the vinculin—talin and vinculin—?-catenin interfaces that have a lifetime of >1000 s at forces up to 10 pN and can last for seconds to tens of seconds at 15 to 25 pN. Our results suggest that these force-bearing intermolecular interfaces provide sufficient mechanical stability to support the vinculin-mediated mechanotransduction at cell-matrix and cell-cell adhesions. Copyright © 2019 The Authors.
Source Title: Science Advances
URI: https://scholarbank.nus.edu.sg/handle/10635/212737
ISSN: 23752548
DOI: 10.1126/sciadv.aav2720
Rights: Attribution-NonCommercial 4.0 International
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