ArticleJournal of molecular biology2011
Actin filament dynamics in the actomyosin VI complex is regulated allosterically by calcium-calmodulin light chain.
Article in Journal of molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
8 citing papers in PubMed, 8 citations in OpenAlex.
- 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
- Two Essential Light Chains Regulate the MyoA Lever Arm To Promote Toxoplasma Gliding Motility.mBio · 2015Article
- Actin age orchestrates myosin-5 and myosin-6 run lengths.Current biology : CB · 2015Article
- Site-specific cation release drives actin filament severing by vertebrate cofilin.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- The spatial structure of cell signaling systems.Physical biology · 2013Article
- Myosin VI in skeletal muscle: its localization in the sarcoplasmic reticulum, neuromuscular junction and muscle nuclei.Histochemistry and cell biology · 2013Article
- The structural dynamics of actin during active interaction with myosin depends on the isoform of the essential light chain.Biochemistry · 2013Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
The contractile and enzymatic activities of myosin VI are regulated by calcium binding to associated calmodulin (CaM) light chains. We have used transient phosphorescence anisotropy to monitor the microsecond rotational dynamics of erythrosin-iodoacetamide-labeled actin with strongly bound myosin VI (MVI) and to evaluate the effect of MVI-bound CaM light chain on actin filament dynamics. MVI binding lowers the amplitude but accelerates actin filament microsecond dynamics in a Ca(2+)- and CaM-dependent manner, as indicated from an increase in the final anisotropy and a decrease in the correlation time of transient phosphorescence anisotropy decays. MVI with bound apo-CaM or Ca(2+)-CaM weakly affects actin filament microsecond dynamics, relative to other myosins (e.g., muscle myosin II and myosin Va). CaM dissociation from bound MVI damps filament rotational dynamics (i.e., increases the torsional rigidity), such that the perturbation is comparable to that induced by other characterized myosins. Analysis of individual actin filament shape fluctuations imaged by fluorescence microscopy reveals a correlated effect on filament bending mechanics. These data support a model in which Ca(2+)-dependent CaM binding to the IQ domain of MVI is linked to an allosteric reorganization of the actin binding site(s), which alters the structural dynamics and the mechanical rigidity of actin filaments. Such modulation of filament dynamics may contribute to the Ca(2)(+)- and CaM-dependent regulation of myosin VI motility and ATP utilization.
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