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

被引：19

作者：

Diensthuber, Ralph P. ^{[1
]}

Mueller, Mirco ^{[1
]}

Heissler, Sarah M. ^{[1
]}

Taft, Manuel H. ^{[1
]}

Chizhov, Igor ^{[1
]}

Manstein, Dietmar J. ^{[1
]}

机构：

[1] Hannover Med Sch, Inst Biophys Chem, Hannover Med Sch, D-30625 Hannover, Germany

来源：

FEBS LETTERS | 2011年 / 585卷 / 05期

关键词：

Non-muscle myosin; Actin; Phalloidin; Allosteric network; FILAMENTS; BINDING; POLYMERIZATION; DYNAMICS; LOOP; DICTYOSTELIUM; STABILIZATION; VISUALIZATION; STABILITY; AFFINITY;

D O I：

10.1016/j.febslet.2011.01.042

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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. (C) 2011 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

引用

页码：767 / 771

页数：5

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