ArticleProceedings of the National Academy of Sciences of the United States of America2006
Mechanics of actomyosin bonds in different nucleotide states are tuned to muscle contraction.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 150 papers.
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Who cites it
150 citing papers in PubMed, 285 citations in OpenAlex.
- Enhanced processivity and collective force production of kinesin-1 at low radial forces.eLife · 2026Article
- Mechanoadaptation via Myosin Cytoplasmic Redistribution Protects Circulating Tumor Cells From Shear-induced Death During Hematogenous Dissemination.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Differential activity of nonmuscle myosin IIA and IIB isoforms generates a dynamic actomyosin network in a concentration-dependent manner.The Journal of biological chemistry · 2026Article
- Crosslinked F-actin networks regulate load-dependent energy conversion.Communications biology · 2026Article
- Mechanoimmunology: past, present, and future perspectives.Mechanobiology in medicine · 2026Review
- Effect of Load on Non-Muscle Myosin 2 Paralog Filaments in a Biomimetic Contractile Actin Array.Small (Weinheim an der Bergstrasse, Germany) · 2026Article
- Enhanced Processivity and Collective Force Production of Kinesin-1 at Low Radial Forces.bioRxiv : the preprint server for biology · 2025Article
- Three types of actomyosin rings within a common cytoplasm exhibit distinct modes of contractility.bioRxiv : the preprint server for biology · 2025Article
- Delayed phosphate release can highly improve energy efficiency of muscle contraction.Biophysical journal · 2025Article
- Dynamic clamping induces rotation-to-beating transition of pinned filaments in gliding assays.Journal of the Royal Society, Interface · 2025Article
- Stomatocyte-discocyte-echinocyte transformations of erythrocyte modulated by membrane-cytoskeleton mechanical properties.Biophysical journal · 2025Article
- Integrin force loading rate in mechanobiology: From model to molecular measurement.QRB discovery · 2025Review
- Single-Molecule Investigation of Load-Dependent Actomyosin Dissociation Kinetics for Cardiac and Slow Skeletal Myosin.Small (Weinheim an der Bergstrasse, Germany) · 2024Article
- Engineering tunable catch bonds with DNA.Nature communications · 2024Article
- FimH-mannose noncovalent bonds survive minutes to hours under force.Biophysical journal · 2024Article
- Mechanical control of antigen detection and discrimination by T and B cell receptors.Biophysical journal · 2024Review
- Mechanical and biochemical feedback combine to generate complex contractile oscillations in cytokinesis.Current biology : CB · 2024Article
- IOP and glaucoma damage: The essential role of optic nerve head and retinal mechanosensors.Progress in retinal and eye research · 2024Review
- 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
- Cardiac desmosomal adhesion relies on ideal-, slip- and catch bonds.Scientific reports · 2024Article
90 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
Muscle contraction and many other cell movements are driven by cyclic interactions between actin filaments and the motor enzyme myosin. Conformational changes in the actin-myosin binding interface occur in concert with the binding of ATP, binding to actin, and loss of hydrolytic by-products, but the effects of these conformational changes on the strength of the actomyosin bond are unknown. The force-dependent kinetics of the actomyosin bond may be particularly important at high loads, where myosin may detach from actin before achieving its full power stroke. Here we show that over a physiological range of rapidly applied loads, actomyosin behaves as a "catch" bond, characterized by increasing lifetimes with increasing loads up to a maximum at approximately 6 pN. Surprisingly, we found that the myosin-ADP bond is possessed of longer lifetimes under load than rigor bonds, although the load at which bond lifetime is maximal remains unchanged. We also found that actomyosin bond lifetime is ultimately dependent not only on load, but loading history as well. These data suggest a complex relationship between the rate of actomyosin dissociation and muscle force and shortening velocity. The 6-pN load for maximum bond lifetime is near the force generated by a single myosin molecule during isometric contraction. This raises the possibility that all catch bonds between load-bearing molecules are "mechanokinetically" tuned to their physiological environment.
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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.