Yao, Mingxi 
ORCID: 0000-0002-3905-8475, Goult, Benjamin T ORCID: 0000-0002-3438-2807, Chen, Hu ORCID: 0000-0002-5958-9361, Cong, Peiwen ORCID: 0000-0001-7753-8368, Sheetz, Michael P and Yan, Jie
(2014)
Mechanical activation of vinculin binding to talin locks talin in an unfolded conformation.
Scientific reports, 4 (1).
4610-.
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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.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | Focal Adhesions, Talin, Vinculin, Surface Plasmon Resonance, Binding Sites, Molecular Conformation, Protein Conformation, Protein Structure, Tertiary, Protein Binding, Protein Folding, Stress, Mechanical, Magnetics, Mechanical Phenomena |
| Divisions: | Faculty of Health and Life Sciences Faculty of Health and Life Sciences > Institute of Systems, Molecular and Integrative Biology |
| Depositing User: | Symplectic Admin |
| Date Deposited: | 13 Mar 2024 09:45 |
| Last Modified: | 13 Mar 2024 09:45 |
| DOI: | 10.1038/srep04610 |
| Related URLs: | |
| URI: | https://livrepository.liverpool.ac.uk/id/eprint/3179333 |
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