May R C
School of Biosciences, University of Birmingham, Edgbaston, United Kingdom.
Cell Mol Life Sci. 2001 Oct;58(11):1607-26. doi: 10.1007/PL00000800.
In recent years the Arp2/3 complex has emerged as a central regulator of actin dynamics, assembling and cross-linking actin filaments to produce a diverse array of cellular structures. Here I discuss our current state of knowledge about this actin-remodelling machine. The predicted structure of the Arp2/3 complex can be directly correlated with its ability to nucleate, cap and cross-link actin filaments. A growing family of Arp2/3 complex activators such as the WASP family, type I myosins, and the newly identified activators cortactin and Abplp tightly regulate this activity within the cell. Localised activation of the Arp2/3 complex produces structures such as lamellipodia or actin patches via a process termed dendritic nucleation. Furthermore, several pathogenic microorganisms have evolved strategies to 'hijack' the Arp2/3 complex to their own advantage. Finally, I discuss some of the questions which remain unanswered about this fascinating complex.
近年来,Arp2/3复合物已成为肌动蛋白动力学的核心调节因子,它组装并交联肌动蛋白丝以产生各种细胞结构。在此,我将讨论我们目前对这种肌动蛋白重塑机器的了解情况。Arp2/3复合物的预测结构与其成核、封端和交联肌动蛋白丝的能力直接相关。越来越多的Arp2/3复合物激活剂家族,如WASP家族、I型肌球蛋白以及新发现的激活剂cortactin和Abplp,在细胞内严格调控这一活性。Arp2/3复合物的局部激活通过一个称为树突状成核的过程产生诸如片状伪足或肌动蛋白斑等结构。此外,几种致病微生物已经进化出策略来“劫持”Arp2/3复合物以使其自身受益。最后,我将讨论一些关于这个迷人复合物仍未得到解答的问题。