Phalloidin, a common reagent for stabilizing actin filaments, perturbs the productive interaction of specific human non-muscle myosin isoforms with F-actin, which may confound in vitro motility assays.
Phalloidin may confound in vitro motility assays with non-muscle myosin-2 isoforms; leaves open effects in cells or other myosins.
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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Diensthuber et al. (2011) studied this question.
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