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Kindlin stabilizes the talin integrin bond under mechanical load by generating an ideal bond

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Aretz,  Jonas
Fässler, Reinhard / Molecular Medicine, Max Planck Institute of Biochemistry, Max Planck Society;

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Fässler,  Reinhard
Fässler, Reinhard / Molecular Medicine, Max Planck Institute of Biochemistry, Max Planck Society;

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Citation

Bodescu, M. A., Aretz, J., Grison, M., Rief, M., & Fässler, R. (2023). Kindlin stabilizes the talin integrin bond under mechanical load by generating an ideal bond. Proceedings of the National Academy of Sciences of the United States of America, 120(26): e2218116120. doi:10.1073/pnas.2218116120.


Cite as: https://hdl.handle.net/21.11116/0000-000D-933F-7
Abstract
Integrin-mediated adhesion is essential for metazoan life. Integrin binding to ligand requires an activation step prior to binding ligand that depends on direct binding of talin and kindlin to the P- integrin cytoplasmic tail and the transmission of force from the actomyosin via talin to the integrin-ligand bonds. However, the affinity of talin for integrin tails is low. It is therefore still unclear how such low-affinity bonds are reinforced to transmit forces up to 10 to 40 pN. In this study, we use single-molecule force spectroscopy by optical tweezers to investigate the mechanical stability of the talin & BULL;integrin bond in the presence and absence of kindlin. While talin and integrin alone form a weak and highly dynamic slip bond, the addition of kindlin- 2 induces a force-independent, ideal talin & BULL;integrin bond, which relies on the steric proximity of and the intervening amino acid sequences between the talin-and kindlin-binding sites in the P-integrin tail. Our findings show how kindlin cooperates with talin to enable transmission of high forces required to stabilize cell adhesion.