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一种由非连续性formin形成肌动蛋白丝束的新机制。

A novel mechanism for the formation of actin-filament bundles by a nonprocessive formin.

作者信息

Michelot Alphée, Derivery Emmanuel, Paterski-Boujemaa Rajaa, Guérin Christophe, Huang Shanjin, Parcy François, Staiger Christopher J, Blanchoin Laurent

机构信息

Departement Réponse et Dynamique Cellulaire, Centre National de la Recherche Scientifique, Institut National de la Recherche Agronomique, Université Joseph Fourier, F38054 Grenoble, France.

出版信息

Curr Biol. 2006 Oct 10;16(19):1924-30. doi: 10.1016/j.cub.2006.07.054.

DOI:10.1016/j.cub.2006.07.054
PMID:17027489
Abstract

Actin-filament bundles (or cables) have a structural role during cell division and morphogenesis, but also serve as important "tracks" for the transport of materials during cytokinesis and polarized cell growth. However, the dynamic formation of these longitudinal actin-filament higher-order structures is not understood. Recently, several lines of evidence suggest that formins provide one avenue for the initiation of actin cables in vivo. A popular model for the mechanism of polymerization of actin filaments by formin involves the processive movement of formin attached at the barbed end of an elongating filament. In the present study, we use an in vitro system to reconstitute the dynamic formation of actin-filament bundles generated by Arabidopsis FORMIN1 (AFH1). To be able to visualize individual events in such a complex system, we used real-time evanescent-wave microscopy. Surprisingly, we find that AFH1 is a nonprocessive formin that moves from the barbed end to the side of an actin filament after the nucleation event. We show why this new mechanism of nucleation by a member of the formin family is important for bundle formation. Finally, we analyze the different parameters controlling the dynamic formation of such longitudinal actin-filament bundles.

摘要

肌动蛋白丝束(或束状结构)在细胞分裂和形态发生过程中具有结构作用,同时在胞质分裂和极化细胞生长过程中也作为物质运输的重要“轨道”。然而,这些纵向肌动蛋白丝高阶结构的动态形成过程尚不清楚。最近,有几条证据表明,formin蛋白为体内肌动蛋白束的起始提供了一条途径。一种关于formin蛋白聚合肌动蛋白丝机制的流行模型涉及附着在伸长丝末端的formin蛋白的连续移动。在本研究中,我们使用体外系统来重建拟南芥formin1(AFH1)产生的肌动蛋白丝束的动态形成过程。为了能够在如此复杂的系统中可视化单个事件,我们使用了实时倏逝波显微镜。令人惊讶的是,我们发现AFH1是一种非连续移动的formin蛋白,在成核事件后从肌动蛋白丝的末端移动到侧面。我们展示了formin家族成员的这种新的成核机制对束状结构形成的重要性。最后,我们分析了控制这种纵向肌动蛋白丝束动态形成的不同参数。

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1
A novel mechanism for the formation of actin-filament bundles by a nonprocessive formin.一种由非连续性formin形成肌动蛋白丝束的新机制。
Curr Biol. 2006 Oct 10;16(19):1924-30. doi: 10.1016/j.cub.2006.07.054.
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Dynamics of the formin for3p in actin cable assembly.肌动蛋白丝束装配过程中formin for3p的动力学
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The formin homology 1 domain modulates the actin nucleation and bundling activity of Arabidopsis FORMIN1.formin同源结构域1调节拟南芥formin1的肌动蛋白成核和束集活性。
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Formins: signaling effectors for assembly and polarization of actin filaments.formin蛋白:肌动蛋白丝组装与极化的信号转导效应分子
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Actin microfilament dynamics and actin side-binding proteins in plants.植物中的肌动蛋白微丝动力学与肌动蛋白侧结合蛋白
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An Arabidopsis class II formin, AtFH19, nucleates actin assembly, binds to the barbed end of actin filaments, and antagonizes the effect of AtFH1 on actin dynamics.拟南芥 II 型formin 蛋白 AtFH19 能起始肌动蛋白组装,结合于肌动蛋白丝的加帽端,并拮抗 AtFH1 对肌动蛋白动力学的影响。
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Processive capping by formin suggests a force-driven mechanism of actin polymerization.Formin介导的持续性加帽表明肌动蛋白聚合存在一种力驱动机制。
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The Diaphanous-related formin dDia2 is required for the formation and maintenance of filopodia.与Diaphanous相关的成束蛋白dDia2是丝状伪足形成和维持所必需的。
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Structural basis of actin filament nucleation and processive capping by a formin homology 2 domain.肌动蛋白丝成核作用及由formin同源结构域2进行的持续性封端的结构基础
Nature. 2005 Feb 3;433(7025):488-94. doi: 10.1038/nature03251. Epub 2005 Jan 5.

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