Chosun University School of Medicine, Department of Cellular and Molecular Medicine, Gwangju 501-759, Korea.
Mol Cells. 2010 Apr;29(4):311-25. doi: 10.1007/s10059-010-0053-8.
The dynamic remolding of the actin cytoskeleton is a critical part of most cellular activities, and malfunction of cytoskeletal proteins results in various human diseases. The transition between two forms of actin, monomeric or G-actin and filamentous or F-actin, is tightly regulated in time and space by a large number of signaling, scaffolding and actin-binding proteins (ABPs). New ABPs are constantly being discovered in the post-genomic era. Most of these proteins are modular, integrating actin binding, protein-protein interaction, membrane-binding, and signaling domains. In response to extracellular signals, often mediated by Rho family GTPases, ABPs control different steps of actin cytoskeleton assembly, including filament nucleation, elongation, severing, capping, and depolymerization. This review summarizes structure-function relationships among ABPs in the regulation of actin cytoskeleton assembly.
肌动蛋白细胞骨架的动态重塑是大多数细胞活动的关键部分,细胞骨架蛋白的功能障碍会导致各种人类疾病。肌动蛋白的两种形式,单体或 G-肌动蛋白和丝状或 F-肌动蛋白之间的转换,通过大量的信号转导、支架和肌动蛋白结合蛋白(ABP)在时间和空间上被紧密调节。在后基因组时代,新的 ABP 不断被发现。这些蛋白质大多数都是模块式的,整合了肌动蛋白结合、蛋白质-蛋白质相互作用、膜结合和信号转导结构域。ABP 可以响应细胞外信号,这些信号通常由 Rho 家族 GTP 酶介导,从而控制肌动蛋白细胞骨架组装的不同步骤,包括丝核的形成、延伸、切断、盖帽和聚合。本文综述了 ABP 在调节肌动蛋白细胞骨架组装中的结构-功能关系。