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Mechanical activation of vinculin binding to talin locks talin in an unfolded conformation
Yao, Mingxi ; Goult, Benjamin T. ; Chen, Hu ; Cong, Peiwen ; Sheetz, Michael P. ; Yan, Jie ; Chen H(陈虎)
刊名http://dx.doi.org/10.1038/srep04610
2014-04-09
关键词ALPHA-ACTININ FORCE REVEALS DYNAMICS DOMAIN AUTOINHIBITION TRANSDUCTION TRANSITION PROTEINS FILAMIN
英文摘要National Research Foundation of Singapore through the Mechanobiology Institute at National University of Singapore; NIH [EB001480]; The force-dependent interaction between talin and vinculin plays a crucial role in the initiation and growth of focal adhesions. Here we use magnetic tweezers to characterise the mechano-sensitive compact N-terminal region of the talin rod, and show that the three helical bundles R1-R3 in this region unfold in three distinct steps consistent with the domains unfolding independently. Mechanical stretching of talin R1-R3 enhances its binding to vinculin and vinculin binding inhibits talin refolding after force is released. Mutations that stabilize R3 identify it as the initial mechano-sensing domain in talin, unfolding at similar to 5 pN, suggesting that 5 pN is the force threshold for vinculin binding and adhesion progression.
语种英语
出版者NATURE PUBLISHING GROUP
内容类型期刊论文
源URL[http://dspace.xmu.edu.cn/handle/2288/92037]  
专题物理技术-已发表论文
推荐引用方式
GB/T 7714
Yao, Mingxi,Goult, Benjamin T.,Chen, Hu,et al. Mechanical activation of vinculin binding to talin locks talin in an unfolded conformation[J]. http://dx.doi.org/10.1038/srep04610,2014.
APA Yao, Mingxi.,Goult, Benjamin T..,Chen, Hu.,Cong, Peiwen.,Sheetz, Michael P..,...&陈虎.(2014).Mechanical activation of vinculin binding to talin locks talin in an unfolded conformation.http://dx.doi.org/10.1038/srep04610.
MLA Yao, Mingxi,et al."Mechanical activation of vinculin binding to talin locks talin in an unfolded conformation".http://dx.doi.org/10.1038/srep04610 (2014).
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