ArticlePLoS computational biology2008
How force might activate talin's vinculin binding sites: SMD reveals a structural mechanism.
Article in PLoS computational biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 86 papers.
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Who cites it
86 citing papers in PubMed, 164 citations in OpenAlex.
- Mechanomedicine: Present state and future promise.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Mechanical Load-Induced Upregulation of Talin2 through Non-Canonical Deubiquitination of OTUB1 Drives Facet Joint Osteoarthritis Pathogenesis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Mechanochemistry: Fundamental Principles and Applications.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Review
- Inhibition of Talin2 dedifferentiates myofibroblasts and reverses lung and kidney fibrosis.Scientific reports · 2025Article
- Article
- Talin2 binds to non-muscle myosin IIa and regulates cell attachment and fibronectin secretion.Scientific reports · 2024Article
- Cellular stiffness sensing through talin 1 in tissue mechanical homeostasis.Science advances · 2024Article
- Molecular dynamics simulations reveal how vinculin refolds partially unfolded talin rod helices to stabilize them against mechanical force.PLoS computational biology · 2024Article
- The focal adhesion protein talin is a mechanically gated A-kinase anchoring protein.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Allosteric activation of vinculin by talin.Nature communications · 2023Article
- Remodeling of the focal adhesion complex by hydrogen-peroxide-induced senescence.Scientific reports · 2023Article
- ConFERMing the role of talin in integrin activation and mechanosignaling.Journal of cell science · 2023Article
- Talin variant P229S compromises integrin activation and associates with multifaceted clinical symptoms.Human molecular genetics · 2022Article
- The mechanical cell - the role of force dependencies in synchronising protein interaction networks.Journal of cell science · 2022Review
- Paxillin: A Hub for Mechano-Transduction from the β3 Integrin-Talin-Kindlin Axis.Frontiers in cell and developmental biology · 2022Review
- Article
- An efficient alpha helix model and simulation framework for stationary electrostatic interaction force estimation.Scientific reports · 2021Article
- Cancer associated talin point mutations disorganise cell adhesion and migration.Scientific reports · 2021Article
- Mechanical Unfolding of Proteins-A Comparative Nonequilibrium Molecular Dynamics Study.Biophysical journal · 2020Article
- Different Vinculin Binding Sites Use the Same Mechanism to Regulate Directional Force Transduction.Biophysical journal · 2020Article
26 more citing papers are in PubMed but not listed here.
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Upon cell adhesion, talin physically couples the cytoskeleton via integrins to the extracellular matrix, and subsequent vinculin recruitment is enhanced by locally applied tensile force. Since the vinculin binding (VB) sites are buried in the talin rod under equilibrium conditions, the structural mechanism of how vinculin binding to talin is force-activated remains unknown. Taken together with experimental data, a biphasic vinculin binding model, as derived from steered molecular dynamics, provides high resolution structural insights how tensile mechanical force applied to the talin rod fragment (residues 486-889 constituting helices H1-H12) might activate the VB sites. Fragmentation of the rod into three helix subbundles is prerequisite to the sequential exposure of VB helices to water. Finally, unfolding of a VB helix into a completely stretched polypeptide might inhibit further binding of vinculin. The first events in fracturing the H1-H12 rods of talin1 and talin2 in subbundles are similar. The proposed force-activated alpha-helix swapping mechanism by which vinculin binding sites in talin rods are exposed works distinctly different from that of other force-activated bonds, including catch bonds.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.