1. Phalloidin perturbs the interaction of human non-muscle myosin isoforms 2A and 2C1 with F-actin
- Author
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Ralph P. Diensthuber, Manuel H. Taft, Dietmar J. Manstein, Igor Chizhov, Sarah M. Heissler, and Mirco Müller
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Gene isoform ,Phalloidine ,Phalloidin ,Biophysics ,macromolecular substances ,Biochemistry ,Filamentous actin ,chemistry.chemical_compound ,Structural Biology ,Myosin ,Genetics ,Non-muscle myosin ,Humans ,Protein Isoforms ,Dictyostelium ,Molecular Biology ,Actin ,Myosin Type II ,Non muscle myosin ,Photolysis ,Myosin Heavy Chains ,biology ,Nonmuscle Myosin Type IIA ,Actin remodeling ,Cell Biology ,Allosteric network ,biology.organism_classification ,Actins ,Cell biology ,Actin Cytoskeleton ,Kinetics ,chemistry ,Protein Binding - Abstract
Phalloidin and fluorescently labeled phalloidin analogs are established reagents to stabilize and mark actin filaments for the investigation of acto-myosin interactions. In the present study, we employed transient and steady-state kinetic measurements as well as in vitro motility assays to show that phalloidin perturbs the productive interaction of human non-muscle myosin-2A and -2C1 with filamentous actin. Phalloidin binding to F-actin results in faster dissociation of the complex formed with non-muscle myosin-2A and -2C1, reduced actin-activated ATP turnover, and slower velocity of actin filaments in the in vitro motility assay. In contrast, phalloidin binding to F-actin does not affect the interaction with human non-muscle myosin isoform 2B and Dictyostelium myosin-2 and myosin-5b.
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