ArticleProceedings of the National Academy of Sciences of the United States of America2014
Plasticity of hydrogen bond networks regulates mechanochemistry of cell adhesion complexes.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 62 citations in OpenAlex.
- A direct computational assessment of vinculin-actin unbinding kinetics reveals catch-bonding behavior.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- A Review of Talin- and Integrin-Dependent Molecular Mechanisms in Cancer Invasion and Metastasis.International journal of molecular sciences · 2025Review
- Engineering tunable catch bonds with DNA.Nature communications · 2024Article
- Theory and Examples of Catch Bonds.The journal of physical chemistry. B · 2024Article
- Topology of molecular deformations induces triphasic catch bonding in selectin-ligand bonds.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Extracellular matrix sensing via modulation of orientational order of integrins and F-actin in focal adhesions.Life science alliance · 2023Article
- 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 · 2023Article
- Catch bonds in sickle cell disease: Shear-enhanced adhesion of red blood cells to laminin.Biophysical journal · 2023Article
- Receptor-Ligand Binding: Effect of Mechanical Factors.International journal of molecular sciences · 2023Review
- Catch bond-inspired hydrogels with repeatable and loading rate-sensitive specific adhesion.Bioactive materials · 2023Article
- Diffusion of a disordered protein on its folded ligand.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Inside-out regulation of E-cadherin conformation and adhesion.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Binding of SARS-CoV-2 Fusion Peptide to Host Endosome and Plasma Membrane.The journal of physical chemistry. B · 2021Article
- Activated nanoscale actin-binding domain motion in the catenin-cadherin complex revealed by neutron spin echo spectroscopy.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Fibrinogen binding is affected by amino acid substitutions in C-terminal repeat region of fibronectin binding protein A.Scientific reports · 2019Article
- Integrins as biomechanical sensors of the microenvironment.Nature reviews. Molecular cell biology · 2019Review
- Regulatory element in fibrin triggers tension-activated transition from catch to slip bonds.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Unraveling the mechanism of the cadherin-catenin-actin catch bond.PLoS computational biology · 2018Article
- Forced-rupture of cell-adhesion complexes reveals abrupt switch between two brittle states.The Journal of chemical physics · 2018Article
- Plasma fibronectin stabilizesProceedings of the National Academy of Sciences of the United States of America · 2017Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Mechanical forces acting on cell adhesion receptor proteins regulate a range of cellular functions by formation and rupture of noncovalent interactions with ligands. Typically, force decreases the lifetimes of intact complexes ("slip bonds"), making the discovery that these lifetimes can also be prolonged ("catch bonds") a surprise. We created a microscopic analytic theory by incorporating the structures of selectin and integrin receptors into a conceptual framework based on the theory of stochastic equations, which quantitatively explains a wide range of experimental data (including catch bonds at low forces and slip bonds at high forces). Catch bonds arise due to force-induced remodeling of hydrogen bond networks, a finding that also accounts for unbinding in structurally unrelated integrin-fibronectin and actomyosin complexes. For the selectin family, remodeling of hydrogen bond networks drives an allosteric transition resulting in the formation of the maximum number of hydrogen bonds determined only by the structure of the receptor and independent of the ligand. A similar transition allows us to predict the increase in the number of hydrogen bonds in a particular allosteric state of α5β1 integrin-fibronectin complex, a conformation which is yet to be crystallized. We also make a testable prediction that a single point mutation (Tyr51Phe) in the ligand associated with selectin should dramatically alter the nature of the catch bond compared with the wild type. Our work suggests that nature uses a ductile network of hydrogen bonds to engineer function over a broad range of forces.
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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.