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肌球蛋白的运动功能:基于肌动蛋白的膜突的来龙去脉。

Myosin motor function: the ins and outs of actin-based membrane protrusions.

机构信息

Department of Cell and Developmental Biology, Vanderbilt University Medical Center, Nashville, TN 37232, USA.

出版信息

Cell Mol Life Sci. 2010 Apr;67(8):1239-54. doi: 10.1007/s00018-009-0254-5. Epub 2010 Jan 27.

Abstract

Cells build plasma membrane protrusions supported by parallel bundles of F-actin to enable a wide variety of biological functions, ranging from motility to host defense. Filopodia, microvilli and stereocilia are three such protrusions that have been the focus of intense biological and biophysical investigation in recent years. While it is evident that actin dynamics play a significant role in the formation of these organelles, members of the myosin superfamily have also been implicated as key players in the maintenance of protrusion architecture and function. Based on a simple analysis of the physical forces that control protrusion formation and morphology, as well as our review of available data, we propose that myosins play two general roles within these structures: (1) as cargo transporters to move critical regulatory components toward distal tips and (2) as mediators of membrane-cytoskeleton adhesion.

摘要

细胞构建由平行 F-肌动蛋白束支撑的质膜突起,以实现各种生物学功能,从运动到宿主防御。近年来,丝状伪足、微绒毛和静纤毛这三种突起成为了生物学和生物物理学研究的焦点。虽然肌动蛋白动力学在这些细胞器的形成中起着重要作用,但肌球蛋白超家族的成员也被认为是维持突起结构和功能的关键因素。基于对控制突起形成和形态的物理力的简单分析,以及对现有数据的回顾,我们提出肌球蛋白在这些结构中发挥两种一般作用:(1)作为货物转运体,将关键调节成分运向远端尖端;(2)作为质膜-细胞骨架黏附的介体。

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引用本文的文献

本文引用的文献

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Cargo binding induces dimerization of myosin VI.货物结合诱导肌球蛋白VI二聚化。
Proc Natl Acad Sci U S A. 2009 Oct 13;106(41):17320-4. doi: 10.1073/pnas.0909748106. Epub 2009 Sep 28.
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Membrane-induced bundling of actin filaments.膜诱导的肌动蛋白丝成束
Nat Phys. 2008 Aug 31;4:789-793. doi: 10.1038/nphys1071.
5
Myosin VI undergoes cargo-mediated dimerization.肌球蛋白VI经历货物介导的二聚化。
Cell. 2009 Aug 7;138(3):537-48. doi: 10.1016/j.cell.2009.05.030.
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Control of cell membrane tension by myosin-I.肌球蛋白-I对细胞膜张力的调控
Proc Natl Acad Sci U S A. 2009 Jul 21;106(29):11972-7. doi: 10.1073/pnas.0901641106. Epub 2009 Jul 2.

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