Abstract.
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 Abp1p 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.
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Received 2 April 2001; received after revision 15 May 2001; accepted 18 May 2001
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May, R. The Arp2/3 complex: a central regulator of the actin cytoskeleton. CMLS, Cell. Mol. Life Sci. 58, 1607–1626 (2001). https://doi.org/10.1007/PL00000800
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DOI: https://doi.org/10.1007/PL00000800