Please use this identifier to cite or link to this item: http://hdl.handle.net/2381/32006
Title: Mechanical activation of vinculin binding to talin locks talin in an unfolded conformation.
Authors: Yao, M.
Goult, Benjamin T.
Chen, H.
Cong, P.
Sheetz, M. P.
Yan, J.
First Published: 2014
Publisher: Nature Publishing Group
Citation: Scientific Reports, 2014, 4:4610
Abstract: 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 ∼5 pN, suggesting that 5 pN is the force threshold for vinculin binding and adhesion progression.
DOI Link: 10.1038/srep04610
ISSN: 2045-2322
eISSN: 2045-2322
Links: http://www.nature.com/srep/2014/140409/srep04610/full/srep04610.html
http://hdl.handle.net/2381/32006
Version: Publisher Version
Status: Peer-reviewed
Type: Journal Article
Rights: This work is licensed under a Creative Commons Attribution-NonCommercialShareAlike 3.0 Unported License (CC BY-NC-SA 3.0). The images in this article are included in the article’s Creative Commons license, unless indicated otherwise in the image credit; if the image is not included under the Creative Commons license, users will need to obtain permission from the license holder in order to reproduce the image. To view a copy of this license, visit http://creativecommons.org/licenses/by-nc-sa/3.0/
Description: PMCID: PMC3980218
Appears in Collections:Published Articles, Dept. of Biochemistry

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