ReviewPhilosophical transactions of the Royal Society of London. Series B, Biological sciences2004
Dynamics of actomyosin interactions in relation to the cross-bridge cycle.
Review in Philosophical transactions of the Royal Society of London. Series B, Biological sciences, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 54 citations in OpenAlex.
- Multiple pathways of the actin-myosin cycle in energy transduction and the release of orthophosphate in muscle.Frontiers in physiology · 2025Review
- Research reviews on myosin head interactions with F-actin.Applied microscopy · 2024Review
- Force and kinetics of fast and slow muscle myosin determined with a synthetic sarcomere-like nanomachine.Communications biology · 2024Article
- Matching Mechanics and Energetics of Muscle Contraction Suggests Unconventional Chemomechanical Coupling during the Actin-Myosin Interaction.International journal of molecular sciences · 2023Article
- Electrostatic interactions in the SH1-SH2 helix of human cardiac myosin modulate the time of strong actomyosin binding.Journal of muscle research and cell motility · 2021Article
- ADisease models & mechanisms · 2017Article
- Mutations in the SH1 helix alter the thermal properties of myosin II.Biophysics and physicobiology · 2017Article
- Poorly understood aspects of striated muscle contraction.BioMed research international · 2015Review
- Magnesium modulates actin binding and ADP release in myosin motors.The Journal of biological chemistry · 2014Article
- Motor proteins and molecular motors: how to operate machines at the nanoscale.Journal of physics. Condensed matter : an Institute of Physics journal · 2013Review
- Direct real-time detection of the actin-activated power stroke within the myosin catalytic domain.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Myosinopathies: pathology and mechanisms.Acta neuropathologica · 2013Review
- Switch II mutants reveal coupling between the nucleotide- and actin-binding regions in myosin V.Biophysical journal · 2012Article
- Expression of the inclusion body myopathy 3 mutation in Drosophila depresses myosin function and stability and recapitulates muscle inclusions and weakness.Molecular biology of the cell · 2012Article
- Moving into the cell: single-molecule studies of molecular motors in complex environments.Nature reviews. Molecular cell biology · 2011Review
- Insights into the importance of hydrogen bonding in the gamma-phosphate binding pocket of myosin: structural and functional studies of serine 236.Biochemistry · 2010Article
- Stabilization of helical order in the thick filaments by blebbistatin: further evidence of coexisting multiple conformations of myosin.Biophysical journal · 2009Article
- Allosteric transitions in biological nanomachines are described by robust normal modes of elastic networks.Current protein & peptide science · 2009Article
- Site-directed spectroscopic probes of actomyosin structural dynamics.Annual review of biophysics · 2009Review
- Dynamics of the nucleotide pocket of myosin measured by spin-labeled nucleotides.Biophysical journal · 2007Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Transient kinetic measurements of the actomyosin ATPase provided the basis of the Lymn-Taylor model for the cross-bridge cycle, which underpins current models of contraction. Following the determination of the structure of the myosin motor domain, it has been possible to introduce probes at defined sites and resolve the steps in more detail. Probes have been introduced in the Dicytostelium myosin II motor domain via three routes: (i) single tryptophan residues at strategic locations throughout the motor domain; (ii) green fluorescent protein fusions at the N and C termini; and (iii) labelled cysteine residues engineered across the actin-binding cleft. These studies are interpreted with reference to motor domain crystal structures and suggest that the tryptophan (W501) in the relay loop senses the lever arm position, which is controlled by the switch 2 open-to-closed transition at the active site. Actin has little effect on this process per se. A mechanism of product release is proposed in which actin has an indirect effect on the switch 2 and lever arm position to achieve mechanochemical coupling. Switch 1 closing appears to be a key step in the nucleotide-induced actin dissociation, while its opening is required for the subsequent activation of product release. This process has been probed with F239W and F242W substitutions in the switch 1 loop. The E706K mutation in skeletal myosin IIa is associated with a human myopathy. To simulate this disease we investigated the homologous mutation, E683K, in the Dictyostelium myosin motor domain.
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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.