Aguda Adeleke H, Burtnick Leslie D, Robinson Robert C
Department of Medical Biochemistry and Microbiology, Uppsala Biomedical Center, Uppsala University, Uppsala 751 23, Sweden.
EMBO Rep. 2005 Mar;6(3):220-6. doi: 10.1038/sj.embor.7400363.
Movement is a defining characteristic of life. Macroscopic motion is driven by the dynamic interactions of myosin with actin filaments in muscle. Directed polymerization of actin behind the advancing membrane of a eukaryotic cell generates microscopic movement. Despite the fundamental importance of actin in these processes, the structure of the actin filament remains unknown. The Holmes model of the actin filament was published 15 years ago, and although it has been widely accepted, no high-resolution structural data have yet confirmed its veracity. Here, we review the implications of recently determined structures of F-actin-binding proteins for the structure of the actin filament and suggest a series of in silico tests for actin-filament models. We also review the significance of these structures for the arp2/3-mediated branched filament.
运动是生命的一个决定性特征。宏观运动是由肌肉中肌球蛋白与肌动蛋白丝的动态相互作用驱动的。真核细胞前进膜后方肌动蛋白的定向聚合产生微观运动。尽管肌动蛋白在这些过程中至关重要,但其丝状体结构仍不为人知。肌动蛋白丝的霍姆斯模型于15年前发表,尽管已被广泛接受,但尚无高分辨率结构数据证实其真实性。在此,我们综述了最近确定的F-肌动蛋白结合蛋白结构对肌动蛋白丝结构的影响,并提出了一系列针对肌动蛋白丝模型的计算机模拟测试。我们还综述了这些结构对arp2/3介导的分支丝的意义。