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https://doi.org/10.1038/ncomms11966
| Title: | The mechanical response of talin | Authors: | Yao M. Goult B.T. Klapholz B. Hu X. Toseland C.P. Guo Y. Cong P. Sheetz M.P. Yan J. |
Keywords: | talin fusion protein glutathione transferase protein binding proteinase talin talin protein, mouse TEV protease adhesion cells and cell components experimental study force kinetics parameterization physiology plasma protein stochasticity Article controlled study force kinetics molecular dynamics nonhuman protein binding protein domain protein expression protein folding protein unfolding simulation velocity animal binding site biomechanics chemistry Escherichia coli gene expression genetics mechanical stress metabolism molecular cloning molecular model mouse procedures protein refolding protein secondary structure single molecule imaging thermodynamics Animals Binding Sites Biomechanical Phenomena Cloning, Molecular Endopeptidases Escherichia coli Gene Expression Glutathione Transferase Kinetics Mice Models, Molecular Protein Binding Protein Folding Protein Interaction Domains and Motifs Protein Refolding Protein Structure, Secondary Recombinant Fusion Proteins Single Molecule Imaging Stress, Mechanical Talin Thermodynamics |
Issue Date: | 2016 | Publisher: | Nature Publishing Group | Citation: | Yao M., Goult B.T., Klapholz B., Hu X., Toseland C.P., Guo Y., Cong P., Sheetz M.P., Yan J. (2016). The mechanical response of talin. Nature Communications 7 : 11966. ScholarBank@NUS Repository. https://doi.org/10.1038/ncomms11966 | Abstract: | Talin, a force-bearing cytoplasmic adapter essential for integrin-mediated cell adhesion, links the actin cytoskeleton to integrin-based cell-extracellular matrix adhesions at the plasma membrane. Its C-terminal rod domain, which contains 13 helical bundles, plays important roles in mechanosensing during cell adhesion and spreading. However, how the structural stability and transition kinetics of the 13 helical bundles of talin are utilized in the diverse talin-dependent mechanosensing processes remains poorly understood. Here we report the force-dependent unfolding and refolding kinetics of all talin rod domains. Using experimentally determined kinetics parameters, we determined the dynamics of force fluctuation during stretching of talin under physiologically relevant pulling speeds and experimentally measured extension fluctuation trajectories. Our results reveal that force-dependent stochastic unfolding and refolding of talin rod domains make talin a very effective force buffer that sets a physiological force range of only a few pNs in the talin-mediated force transmission pathway. © 2016 The Author(s). | Source Title: | Nature Communications | URI: | https://scholarbank.nus.edu.sg/handle/10635/174949 | ISSN: | 20411723 | DOI: | 10.1038/ncomms11966 |
| Appears in Collections: | Elements Staff Publications |
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