The mechanical response of talin
Copyright policy )The mechanical response of talin
AbstractTalin, 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.
- National University of Singapore Singapore
- National University of Singapore Libraries Singapore
- King’s University United States
- University of Cambridge United Kingdom
- Wellcome / CRUK Gurdon Institute United Kingdom
molecular cloning, Models, Molecular, Talin, Protein Folding, protein refolding, Gene Expression, protein binding, Protein Refolding, Protein Structure, Secondary, Mice, protein folding, glutathione transferase, animal, genetics, Cloning, Molecular, Glutathione Transferase, protein unfolding, Q, protein domain, simulation, parameterization, Single Molecule Imaging, Biomechanical Phenomena, adhesion, proteinase, Structural biology, force, Protein Binding, velocity, Science, Recombinant Fusion Proteins, chemistry, experimental study, biomechanics, Article, thermodynamics, QH301, talin protein, Endopeptidases, fusion protein, Escherichia coli, Animals, TEV protease, controlled study, Protein Interaction Domains and Motifs, procedures, protein expression, mouse, plasma, stochasticity, nonhuman, Binding Sites, binding site, talin, mechanical stress, molecular dynamics, Kinetics, kinetics, single molecule imaging, physiology, gene expression, protein secondary structure, Stress, Mechanical, cells and cell components, molecular model, protein, metabolism
molecular cloning, Models, Molecular, Talin, Protein Folding, protein refolding, Gene Expression, protein binding, Protein Refolding, Protein Structure, Secondary, Mice, protein folding, glutathione transferase, animal, genetics, Cloning, Molecular, Glutathione Transferase, protein unfolding, Q, protein domain, simulation, parameterization, Single Molecule Imaging, Biomechanical Phenomena, adhesion, proteinase, Structural biology, force, Protein Binding, velocity, Science, Recombinant Fusion Proteins, chemistry, experimental study, biomechanics, Article, thermodynamics, QH301, talin protein, Endopeptidases, fusion protein, Escherichia coli, Animals, TEV protease, controlled study, Protein Interaction Domains and Motifs, procedures, protein expression, mouse, plasma, stochasticity, nonhuman, Binding Sites, binding site, talin, mechanical stress, molecular dynamics, Kinetics, kinetics, single molecule imaging, physiology, gene expression, protein secondary structure, Stress, Mechanical, cells and cell components, molecular model, protein, metabolism
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