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|Title:||Direct single-molecule quantification reveals unexpectedly high mechanical stability of vinculin—talin/?-catenin linkages||Authors:||Le, S.
|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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