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Mechanical activation of vinculin binding to talin locks talin in an unfolded conformation

Year: 2014
Type: article
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: 10.1038/srep04610
Authors: Mingxi Yao, Benjamin T. Goult, Hu Chen, Peiwen Cong, Michael P. Sheetz, Jie Yan
Institutions: National University of Singapore, Mechanobiology Institute, University of Leicester, Xiamen University, Singapore-MIT Alliance for Research and Technology, Columbia University
Language: English
Subfield: Cell Biology
Open Access status: gold
Estimated APC paid: $2,690
Funders: National Research Foundation, National University of Singapore, National Research Foundation Singapore, Mechanobiology Institute, Singapore, National Institutes of Health, National Institute of Biomedical Imaging and Bioengineering
OpenAlex ID: W2085117752
FWCI: 11.23
Cites: 36
Cited by: 372
Related to: 10