ArticleEuropean biophysics journal : EBJ2012
Cooperative regulation of myosin-S1 binding to actin filaments by a continuous flexible Tm-Tn chain.
Article in European biophysics journal : EBJ, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 43 citations in OpenAlex.
- The elementary step that generates force and sinusoidal analysis in striated muscle fibers.Journal of muscle research and cell motility · 2025Review
- Changing face of contractile activation in striated muscle at physiological temperature.The Journal of general physiology · 2023Article
- Using Multiscale Simulations as a Tool to Interpret Equatorial X-ray Fiber Diffraction Patterns from Skeletal Muscle.International journal of molecular sciences · 2023Article
- Effect of Myosin Isoforms on Cardiac Muscle Twitch of Mice, Rats and Humans.International journal of molecular sciences · 2022Article
- The effect of variable troponin C mutation thin filament incorporation on cardiac muscle twitch contractions.Journal of molecular and cellular cardiology · 2021Article
- Multiscale modeling of twitch contractions in cardiac trabeculae.The Journal of general physiology · 2021Article
- Troponin Revealed: Uncovering the Structure of the Thin Filament On-Off Switch in Striated Muscle.Biophysical journal · 2021Review
- A new twist on tropomyosin binding to actin filaments: perspectives on thin filament function, assembly and biomechanics.Journal of muscle research and cell motility · 2020Review
- A Stochastic Multiscale Model of Cardiac Thin Filament Activation Using Brownian-Langevin Dynamics.Biophysical journal · 2019Article
- The mechanism of thin filament regulation: Models in conflict?The Journal of general physiology · 2019Review
- Tropomyosin dynamics during cardiac muscle contraction as governed by a multi-well energy landscape.Progress in biophysics and molecular biology · 2019Article
- Computational Tool to Study Perturbations in Muscle Regulation and Its Application to Heart Disease.Biophysical journal · 2019Article
- Microscopic heat pulses activate cardiac thin filaments.The Journal of general physiology · 2019Article
- Nebulin and titin modulate cross-bridge cycling and length-dependent calcium sensitivity.The Journal of general physiology · 2019Article
- Modeling the Actin.myosin ATPase Cross-Bridge Cycle for Skeletal and Cardiac Muscle Myosin Isoforms.Biophysical journal · 2017Article
- Actomyosin based contraction: one mechanokinetic model from single molecules to muscle?Journal of muscle research and cell motility · 2016Article
- Investigating the effects of tropomyosin mutations on its flexibility and interactions with filamentous actin using molecular dynamics simulation.Journal of muscle research and cell motility · 2016Article
- Structural determinants of muscle thin filament cooperativity.Archives of biochemistry and biophysics · 2016Review
- Predicting Effects of Tropomyosin Mutations on Cardiac Muscle Contraction through Myofilament Modeling.Frontiers in physiology · 2016Article
- Direct Measurements of Local Coupling between Myosin Molecules Are Consistent with a Model of Muscle Activation.PLoS computational biology · 2015Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
Abstract
The regulation of striated muscle contraction involves cooperative interactions between actin filaments, myosin-S1 (S1), tropomyosin (Tm), troponin (Tn), and calcium. These interactions are modeled by treating overlapping tropomyosins as a continuous flexible chain (CFC), weakly confined by electrostatic interactions with actin. The CFC is displaced locally in opposite directions on the actin surface by the binding of either S1 or Troponin I (TnI) to actin. The apparent rate constants for myosin and TnI binding to and detachment from actin are then intrinsically coupled via the CFC model to the presence of neighboring bound S1s and TnIs. Monte Carlo simulations at prescribed values of the CFC stiffness, the CFC's degree of azimuthal confinement, and the angular displacements caused by the bound proteins were able to predict the stopped-flow transients of S1 binding to regulated F-actin. The transients collected over a large range of calcium concentrations could be well described by adjusting a single calcium-dependent parameter, the rate constant of TnI detachment from actin, k(-I). The resulting equilibrium constant K(B) ≡ 1/K(I) varied sigmoidally with the free calcium, increasing from 0.12 at low calcium (pCa >7) to 12 at high calcium (pCa <5.5) with a Hill coefficient of ~2.15. The similarity of the curves for excess-actin and excess-myosin data confirms their allosteric relationship. The spatially explicit calculations confirmed variable sizes for the cooperative units and clustering of bound myosins at low calcium concentrations. Moreover, inclusion of negative cooperativity between myosin units predicted the observed slowing of myosin binding at excess-myosin concentrations.
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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.