Actin filaments (F-actin) are a key component of eukaryotic cells. Whether serving as a scaffold for myosin or using their polymerization to push onto cellular components, their function is always related to force generation. To control and fine-tune force production, cells have a large array of actin-binding proteins (ABPs) dedicated to control every aspect of actin polymerization, filament localization, and their overall mechanical properties. Although great advances have been made in our biochemical understanding of the remodeling of the actin cytoskeleton, the structural basis of this process is still being deciphered. In this review, we summarize our current understanding of this process. We outline how ABPs control the nucleation and disassembly, and how these processes are affected by the nucleotide state of the filaments. In addition, we highlight recent advances in the understanding of actomyosin force generation, and describe recent advances brought forward by the developments of electron cryomicroscopy.

中文翻译：

---

对肌动蛋白细胞骨架重塑的结构理解。

肌动蛋白丝（F-肌动蛋白）是真核细胞的关键组成部分。无论是用作肌球蛋白的支架还是利用其聚合作用推向细胞组分，其功能始终与力的产生有关。为了控制和微调力的产生，细胞具有大量的肌动蛋白结合蛋白（ABP），专门用于控制肌动蛋白聚合，细丝定位及其整体机械性能的各个方面。尽管我们对肌动蛋白细胞骨架重塑的生化理解取得了很大进展，但该过程的结构基础仍在研究中。在这篇评论中，我们总结了我们目前对该过程的理解。我们概述了ABP如何控制成核和分解，以及这些过程如何受到细丝核苷酸状态的影响。此外，