ArticleBiophysical journal2012
Structural states and dynamics of the D-loop in actin.
Article in Biophysical journal, 2012. 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.
- Highly divergent apicomplexan cytoskeletons provide additional models for actin biology.The FEBS journal · 2025Review
- Protein design of two-component tubular assemblies similar to cytoskeletons.Nature communications · 2025Article
- Structural basis of MICAL autoinhibition.Nature communications · 2024Article
- Cracked actin filaments as mechanosensitive receptors.Biophysical journal · 2024Article
- High-resolution yeast actin structures indicate the molecular mechanism of actin filament stiffening by cations.Communications chemistry · 2024Article
- Study of the Myosin Relay Helix Peptide by Molecular Dynamics Simulations, Pump-Probe and 2D Infrared Spectroscopy.International journal of molecular sciences · 2024Article
- MICAL-mediated oxidation of actin and its effects on cytoskeletal and cellular dynamics.Frontiers in cell and developmental biology · 2023Review
- Structural basis for tunable control of actin dynamics by myosin-15 in mechanosensory stereocilia.Science advances · 2022Article
- Structural basis of rapid actin dynamics in the evolutionarily divergent Leishmania parasite.Nature communications · 2022Article
- Magic angle spinning NMR structure of human cofilin-2 assembled on actin filaments reveals isoform-specific conformation and binding mode.Nature communications · 2022Article
- A high-throughput fluorescence lifetime-based assay to detect binding of myosin-binding protein C to F-actin.The Journal of general physiology · 2021Article
- Article
- Overexpression of Lifeact-GFP Disrupts F-Actin Organization in Cardiomyocytes and Impairs Cardiac Function.Frontiers in cell and developmental biology · 2021Article
- Structural basis for polarized elongation of actin filaments.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Insights into Actin Polymerization and Nucleation Using a Coarse-Grained Model.Biophysical journal · 2020Article
- The Disordered Cellular Multi-Tasker WIP and Its Protein-Protein Interactions: A Structural View.Biomolecules · 2020Review
- Towards a structural understanding of the remodeling of the actin cytoskeleton.Seminars in cell & developmental biology · 2020Review
- D-Loop Mutation G42A/G46A Decreases Actin Dynamics.Biomolecules · 2020Article
- D-loop Dynamics and Near-Atomic-Resolution Cryo-EM Structure of Phalloidin-Bound F-Actin.Structure (London, England : 1993) · 2020Article
- ADF/cofilin regulation from a structural viewpoint.Journal of muscle research and cell motility · 2020Review
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
Conformational changes induced by ATP hydrolysis on actin are involved in the regulation of complex actin networks. Previous structural and biochemical data implicate the DNase I binding loop (D-loop) of actin in such nucleotide-dependent changes. Here, we investigated the structural and conformational states of the D-loop (in solution) using cysteine scanning mutagenesis and site-directed labeling. The reactivity of D-loop cysteine mutants toward acrylodan and the mobility of spin labels on these mutants do not show patterns of an α-helical structure in monomeric and filamentous actin, irrespective of the bound nucleotide. Upon transition from monomeric to filamentous actin, acrylodan emission spectra and electron paramagnetic resonance line shapes of labeled mutants are blue-shifted and more immobilized, respectively, with the central residues (residues 43-47) showing the most drastic changes. Moreover, complex electron paramagnetic resonance line shapes of spin-labeled mutants suggest several conformational states of the D-loop. Together with a new (to our knowledge) actin crystal structure that reveals the D-loop in a unique hairpin conformation, our data suggest that the D-loop equilibrates in F-actin among different conformational states irrespective of the nucleotide state of actin.
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