Abstract:
:α-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 α-actinin 1 using magnetic tweezers, we determined the mechanical stability and kinetics of the functional domains in α-actinin 1. Moreover, we identified the force-dependence of vinculin binding to α-actinin 1, with the demonstration that force is required to expose the high-affinity binding site for vinculin binding. Further, a role of the α-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 α-actinin 1, which sheds important light on the molecular mechanisms underlying its mechanotransmission and mechanosensing functions.
journal_name
Cell Repjournal_title
Cell reportsauthors
Le S,Hu X,Yao M,Chen H,Yu M,Xu X,Nakazawa N,Margadant FM,Sheetz MP,Yan Jdoi
10.1016/j.celrep.2017.11.040subject
Has Abstractpub_date
2017-12-05 00:00:00pages
2714-2723issue
10issn
2211-1247pii
S2211-1247(17)31677-7journal_volume
21pub_type
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