ArticleJournal of molecular biology2010
Myosin isoform determines the conformational dynamics and cooperativity of actin filaments in the strongly bound actomyosin complex.
Article in Journal of molecular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 47 citations in OpenAlex.
- Actin's functional "switch": Constraining C-terminal conformational flexibility disrupts functionally important communication networks.The Journal of biological chemistry · 2026Article
- Molecular mechanisms of hotspot variants in cytoskeletal β-actin associated with Baraitser-Winter syndrome.The FEBS journal · 2025Article
- Multiple Mechanisms to Regulate Actin Functions: "Fundamental" Versus Lineage-Specific Mechanisms and Hierarchical Relationships.Biomolecules · 2025Review
- Nano-Scale Video Imaging of Motility Machinery by High-Speed Atomic Force Microscopy.Biomolecules · 2025Review
- Cooperative ligand binding to a double-stranded Ising lattice-Application to cofilin binding to actin filaments.PNAS nexus · 2023Article
- Cooperativity of myosin II motors in the non-regulated and regulated thin filaments investigated with high-speed AFM.The Journal of general physiology · 2023Article
- Actin-binding domain of Rng2 sparsely bound on F-actin strongly inhibits actin movement on myosin II.Life science alliance · 2023Article
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- High-throughput screen, using time-resolved FRET, yields actin-binding compounds that modulate actin-myosin structure and function.The Journal of biological chemistry · 2018Article
- Article
- Phosphomimetic S3D cofilin binds but only weakly severs actin filaments.The Journal of biological chemistry · 2017Article
- Article
- Myosin-Induced Gliding Patterns at Varied [MgATP] Unveil a Dynamic Actin Filament.Biophysical journal · 2016Article
- Cofilin-induced cooperative conformational changes of actin subunits revealed using cofilin-actin fusion protein.Scientific reports · 2016Article
- Actin age orchestrates myosin-5 and myosin-6 run lengths.Current biology : CB · 2015Article
- High-resolution helix orientation in actin-bound myosin determined with a bifunctional spin label.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
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- Article
- Redox-sensitive residue in the actin-binding interface of myosin.Biochemical and biophysical research communications · 2014Article
- Single-molecule imaging and kinetic analysis of cooperative cofilin-actin filament interactions.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
We used transient phosphorescence anisotropy to detect the microsecond rotational dynamics of erythrosin-iodoacetamide-labeled actin strongly bound to single-headed fragments of muscle myosin subfragment 1 (S1) and non-muscle myosin V (MV). The conformational dynamics of actin filaments in solution are markedly influenced by the isoform of bound myosin. Both myosins increase the final anisotropy of actin at substoichiometric binding densities, indicating long-range, non-nearest neighbor cooperative restriction of filament rotational dynamics amplitude, but the cooperative unit is larger with MV than with muscle S1. Both myosin isoforms also cooperatively affect the actin filament rotational correlation time, but with opposite effects: muscle S1 decreases rates of intrafilament torsional motion, while binding of MV increases the rates of motion. The cooperative effects on the rates of intrafilament motions correlate with the kinetics of myosin binding to actin filaments such that MV binds more rapidly and muscle myosin binds more slowly to partially decorated filaments than to bare filaments. The two isoforms also differ in their effects on the phosphorescence lifetime of the actin-bound erythrosin iodoacetamide: while muscle S1 increases the lifetime, suggesting decreased aqueous exposure of the probe, MV does not induce a significant change. We conclude that the dynamics and structure of actin in the strongly bound actomyosin complex are determined by the isoform of the bound myosin in a manner likely to accommodate the diverse functional roles of actomyosin in muscle and non-muscle cells.
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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.