Academic Journal

Structural basis of αE-catenin–F-actin catch bond behavior

التفاصيل البيبلوغرافية
العنوان: Structural basis of αE-catenin–F-actin catch bond behavior
المؤلفون: Xiao-Ping Xu, Sabine Pokutta, Megan Torres, Mark F Swift, Dorit Hanein, Niels Volkmann, William I Weis
المصدر: eLife, Vol 9 (2020)
بيانات النشر: eLife Sciences Publications Ltd, 2020.
سنة النشر: 2020
المجموعة: LCC:Medicine
LCC:Science
LCC:Biology (General)
مصطلحات موضوعية: alphae-catenin, actin, vinculin, catch bond, adherens junction, cryo-EM, Medicine, Science, Biology (General), QH301-705.5
الوصف: Cell-cell and cell-matrix junctions transmit mechanical forces during tissue morphogenesis and homeostasis. α-Catenin links cell-cell adhesion complexes to the actin cytoskeleton, and mechanical load strengthens its binding to F-actin in a direction-sensitive manner. Specifically, optical trap experiments revealed that force promotes a transition between weak and strong actin-bound states. Here, we describe the cryo-electron microscopy structure of the F-actin-bound αE-catenin actin-binding domain, which in solution forms a five-helix bundle. In the actin-bound structure, the first helix of the bundle dissociates and the remaining four helices and connecting loops rearrange to form the interface with actin. Deletion of the first helix produces strong actin binding in the absence of force, suggesting that the actin-bound structure corresponds to the strong state. Our analysis explains how mechanical force applied to αE-catenin or its homolog vinculin favors the strongly bound state, and the dependence of catch bond strength on the direction of applied force.
نوع الوثيقة: article
وصف الملف: electronic resource
اللغة: English
تدمد: 2050-084X
Relation: https://elifesciences.org/articles/60878; https://doaj.org/toc/2050-084X
DOI: 10.7554/eLife.60878
URL الوصول: https://doaj.org/article/7ef2fe8caae548c5b3d264ed5636d68d
رقم الانضمام: edsdoj.7ef2fe8caae548c5b3d264ed5636d68d
قاعدة البيانات: Directory of Open Access Journals
الوصف
تدمد:2050084X
DOI:10.7554/eLife.60878