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FEBS Lett. 2011 Mar 9;585(5):767-71. doi: 10.1016/j.febslet.2011.01.042. Epub 2011 Feb 3.

Phalloidin perturbs the interaction of human non-muscle myosin isoforms 2A and 2C1 with F-actin.

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Institute for Biophysical Chemistry, Hannover Medical School, Germany.


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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