ArticleThe Journal of biological chemistry2011
Regulation of catch bonds by rate of force application.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
What it found
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Who cites it
27 citing papers in PubMed, 50 citations in OpenAlex.
- Mechanotransduction through T cell receptors: consensus, controversies and future outlooks.Experimental & molecular medicine · 2026Review
- Mechanical forces amplify TCR mechanotransduction in T cell activation and function.Applied physics reviews · 2024Review
- Emergence of slip-ideal-slip behavior in tip-links serve as force filters of sound in hearing.Nature communications · 2024Article
- What's the Catch? The Significance of Catch Bonds in T Cell Activation.Journal of immunology (Baltimore, Md. : 1950) · 2023Review
- Immune-mediated alopecias and their mechanobiological aspects.Cells & development · 2022Review
- Mechanosensitive axon outgrowth mediated by L1-laminin clutch interface.Biophysical journal · 2021Article
- Single-molecule investigations of T-cell activation.Current opinion in biomedical engineering · 2019Article
- Dynamic bonds and their roles in mechanosensing.Current opinion in chemical biology · 2019Review
- Fast Force Loading Disrupts Molecular Binding Stability in Human and Mouse Cell Adhesions.Molecular & cellular biomechanics : MCB · 2019Article
- Exploring the Sulfatase 1 Catch Bond Free Energy Landscape using Jarzynski's Equality.Scientific reports · 2018Article
- Role of Mechanotransduction and Tension in T Cell Function.Frontiers in immunology · 2018Review
- Mechanical forces in the immune system.Nature reviews. Immunology · 2017Review
- Automated Dielectrophoretic Tweezers-Based Force Spectroscopy System in a Microfluidic Device.Sensors (Basel, Switzerland) · 2017Article
- Amino acid polymorphisms in the fibronectin-binding repeats of fibronectin-binding protein A affect bond strength and fibronectin conformation.The Journal of biological chemistry · 2017Article
- Phenomenological and microscopic theories for catch bonds.Journal of structural biology · 2017Article
- A model for cyclic mechanical reinforcement.Scientific reports · 2016Article
- Stiff substrates enhance monocytic cell capture through E-selectin but not P-selectin.Integrative biology : quantitative biosciences from nano to macro · 2016Article
- Catch bond interaction between cell-surface sulfatase Sulf1 and glycosaminoglycans.Biophysical journal · 2015Article
- Probing time-dependent mechanical behaviors of catch bonds based on two-state models.Scientific reports · 2015Article
- Accumulation of serial forces on TCR and CD8 frequently applied by agonist antigenic peptides embedded in MHC molecules triggers calcium in T cells.Journal of immunology (Baltimore, Md. : 1950) · 2014Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
The current paradigm for receptor-ligand dissociation kinetics assumes off-rates as functions of instantaneous force without impact from its prior history. This a priori assumption is the foundation for predicting dissociation from a given initial state using kinetic equations. Here we have invalidated this assumption by demonstrating the impact of force history with single-bond kinetic experiments involving selectins and their ligands that mediate leukocyte tethering and rolling on vascular surfaces during inflammation. Dissociation of bonds between L-selectin and P-selectin glycoprotein ligand-1 (PSGL-1) loaded at a constant ramp rate to a constant hold force behaved as catch-slip bonds at low ramp rates that transformed to slip-only bonds at high ramp rates. Strikingly, bonds between L-selectin and 6-sulfo-sialyl Lewis X were impervious to ramp rate changes. This ligand-specific force history effect resembled the effect of a point mutation at the L-selectin surface (L-selectinA108H) predicted to contact the former but not the latter ligand, suggesting that the high ramp rate induced similar structural changes as the mutation. Although the A108H substitution in L-selectin eliminated the ramp rate responsiveness of its dissociation from PSGL-1, the inverse mutation H108A in P-selectin acquired the ramp rate responsiveness. Our data are well explained by the sliding-rebinding model for catch-slip bonds extended to incorporate the additional force history dependence, with Ala-108 playing a pivotal role in this structural mechanism. These results call for a paradigm shift in modeling the mechanical regulation of receptor-ligand bond dissociation, which includes conformational coupling between binding pocket and remote regions of the interacting molecules.
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Registered trials
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.