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

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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Diensthuber RP,Müller M,Heissler SM,Taft MH,Chizhov I,Manstein DJ

doi

10.1016/j.febslet.2011.01.042

subject

Has Abstract

pub_date

2011-03-09 00:00:00

pages

767-71

issue

5

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(11)00079-2

journal_volume

585

pub_type

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