An ensemble of flexible conformations underlies mechanotransduction by the cadherin–catenin adhesion complex. Bush, M., Alhanshali, B. M., Qian, S., Stanley, C. B., Heller, W. T., Matsui, T., Weiss, T. M., Nicholl, I. D., Walz, T., Callaway, D. J. E., & Bu, Z. Proceedings of the National Academy of Sciences, 116(43):21545–21555, October, 2019. Publisher: National Academy of Sciences Section: Biological Sciences![An ensemble of flexible conformations underlies mechanotransduction by the cadherin–catenin adhesion complex [link]](https://bibbase.org/img/filetypes/link.svg "link")
Paper doi abstract bibtex The cadherin–catenin adhesion complex is the central component of the cell–cell adhesion adherens junctions that transmit mechanical stress from cell to cell. We have determined the nanoscale structure of the adherens junction complex formed by the α-catenin•β-catenin•epithelial cadherin cytoplasmic domain (ABE) using negative stain electron microscopy, small-angle X-ray scattering, and selective deuteration/small-angle neutron scattering. The ABE complex is highly pliable and displays a wide spectrum of flexible structures that are facilitated by protein-domain motions in α- and β-catenin. Moreover, the 107-residue intrinsically disordered N-terminal segment of β-catenin forms a flexible “tongue” that is inserted into α-catenin and participates in the assembly of the ABE complex. The unanticipated ensemble of flexible conformations of the ABE complex suggests a dynamic mechanism for sensitivity and reversibility when transducing mechanical signals, in addition to the catch/slip bond behavior displayed by the ABE complex under mechanical tension. Our results provide mechanistic insight into the structural dynamics for the cadherin–catenin adhesion complex in mechanotransduction.
@article{bush_ensemble_2019,
title = {An ensemble of flexible conformations underlies mechanotransduction by the cadherin–catenin adhesion complex},
volume = {116},
copyright = {Copyright © 2019 the Author(s). Published by PNAS.. https://creativecommons.org/licenses/by-nc-nd/4.0/This open access article is distributed under Creative Commons Attribution-NonCommercial-NoDerivatives License 4.0 (CC BY-NC-ND).},
issn = {0027-8424, 1091-6490},
url = {https://www.pnas.org/content/116/43/21545},
doi = {10.1073/pnas.1911489116},
abstract = {The cadherin–catenin adhesion complex is the central component of the cell–cell adhesion adherens junctions that transmit mechanical stress from cell to cell. We have determined the nanoscale structure of the adherens junction complex formed by the α-catenin•β-catenin•epithelial cadherin cytoplasmic domain (ABE) using negative stain electron microscopy, small-angle X-ray scattering, and selective deuteration/small-angle neutron scattering. The ABE complex is highly pliable and displays a wide spectrum of flexible structures that are facilitated by protein-domain motions in α- and β-catenin. Moreover, the 107-residue intrinsically disordered N-terminal segment of β-catenin forms a flexible “tongue” that is inserted into α-catenin and participates in the assembly of the ABE complex. The unanticipated ensemble of flexible conformations of the ABE complex suggests a dynamic mechanism for sensitivity and reversibility when transducing mechanical signals, in addition to the catch/slip bond behavior displayed by the ABE complex under mechanical tension. Our results provide mechanistic insight into the structural dynamics for the cadherin–catenin adhesion complex in mechanotransduction.},
language = {en},
number = {43},
urldate = {2020-04-12},
journal = {Proceedings of the National Academy of Sciences},
author = {Bush, Martin and Alhanshali, Bashir M. and Qian, Shuo and Stanley, Christopher B. and Heller, William T. and Matsui, Tsutomu and Weiss, Thomas M. and Nicholl, Iain D. and Walz, Thomas and Callaway, David J. E. and Bu, Zimei},
month = oct,
year = {2019},
pmid = {31591245},
note = {Publisher: National Academy of Sciences
Section: Biological Sciences},
keywords = {adherens junction, mechanotransduction, negative stain electron microscopy, small-angle X-ray scattering, small-angle neutron scattering},
pages = {21545--21555}
}
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