期刊
CELL REPORTS
卷 21, 期 10, 页码 2714-2723出版社
CELL PRESS
DOI: 10.1016/j.celrep.2017.11.040
关键词
-
类别
资金
- National Research Foundation, Prime Minister's Office, Singapore, under its NRF Investigatorship Programme (NRF Investigatorship Award) [NRF-NRFI2016-03]
- National Research Foundation through the Mechanobiology Institute Singapore
- Human Frontier Science Program [RGP00001/2016]
alpha-Actinins, a family of critical cytoskeletal actin-binding proteins that usually exist as anti-parallel dimers, play crucial roles in organizing the framework of the cytoskeleton through crosslinking the actin filaments, as well as in focal adhesion maturation. However, the molecular mechanisms underlying its functions are unclear. Here, by mechanical manipulation of single human a-actinin 1 using magnetic tweezers, we determined the mechanical stability and kinetics of the functional domains in a-actinin 1. Moreover, we identified the force-dependence of vinculin binding to a-actinin 1, with the demonstration that force is required to expose the high-affinity binding site for vinculin binding. Further, a role of the a-actinin 1 as molecular shock absorber for the cytoskeleton network is revealed. Our results provide a comprehensive analysis of the force-dependent stability and interactions of a-actinin 1, which sheds important light on the molecular mechanisms underlying its mechanotransmission and mechanosensing functions.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据