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肌动蛋白-espin系统的结构多态性:静纤毛中细丝和连接蛋白的典型系统。

Structural polymorphism of the actin-espin system: a prototypical system of filaments and linkers in stereocilia.

作者信息

Purdy Kirstin R, Bartles James R, Wong Gerard C L

机构信息

Department of Materials Science and Engineering, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801, USA.

出版信息

Phys Rev Lett. 2007 Feb 2;98(5):058105. doi: 10.1103/PhysRevLett.98.058105. Epub 2007 Feb 1.

Abstract

We examine the interaction between cytoskeletal F-actin and espin 3A, a prototypical actin bundling protein found in sensory cell microvilli, including ear cell stereocilia. Espin induces twist distortions in F-actin as well as facilitates bundle formation. Mutations in one of the two F-actin binding sites of espin, which have been implicated in deafness, can tune espin-actin interactions and radically transform the system's phase behavior. These results are compared to recent theoretical work on the general phase behavior linker-rod systems.

摘要

我们研究了细胞骨架F-肌动蛋白与espin 3A之间的相互作用,espin 3A是一种在感觉细胞微绒毛(包括耳细胞静纤毛)中发现的典型肌动蛋白成束蛋白。Espin会在F-肌动蛋白中引起扭曲变形,并促进肌动蛋白束的形成。Espin的两个F-肌动蛋白结合位点之一发生的突变与耳聋有关,这些突变可以调节espin-肌动蛋白的相互作用,并从根本上改变系统的相行为。我们将这些结果与最近关于一般相行为连接棒系统的理论研究进行了比较。

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