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Cell motility

Actin branches out

Nature volume 394, pages 125–126 (1998)Cite this article

The ability of cells to move is essential for the development and survival of multicellular organisms, yet it can also be detrimental — when cancer cells migrate to distant parts of the body and colonize new tumours, for example. Cell movement is thought to be driven largely by the polymerization of actin monomers into filaments near the plasma membrane, and by the contractile forces of myosin motors found deeper in the cell. Although the mechanism of muscle contraction is fairly well understood, we still don't know much about the roles of actin and myosin in cell migration. But reports by Mullins et al.1 in Proceedings of the National Academy of Sciences and Welch et al.2 in Science reveal that a seven-protein complex is central in organizing actin structures. This complex contains the actin-related proteins Arp2 and Arp3, and has been thrust into the spotlight because it may initiate and organize protrusion of an actin-based dynamic meshwork into thin sheets (lamellipodia) or spikes (filopodia).

First identified in Acanthamoeba3, the Arp2/3 complex is conserved from yeast to mammals. In fibroblasts and amoebas, this complex is localized at the leading edge of cells — the ideal position to initiate the polymerization of actin that is required for cell motility. However, the Arp2/3 complex is not found in the more stable actin-myosin bundles that are normally associated with adhesion and contraction4,5,6. In budding yeast, the Arp2/3 complex is required for motility of the cortical actin patches (dynamic, actin-rich structures that may be analogous to mammalian cortical actin) in which it is found7,8. It is also the only known host-encoded factor that can induce actin polymerization on the surface of the motile intracellular pathogen Listeria monocytogenes9.

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Figure 1: Structure of an actin filament.
Figure 2: Dendritic-nucleation model for protrusion of lamellipodia.
Figure 3: Electron micrograph showing actin filaments and bundles in the lamellipodium of a fibroblast.

D. MULLINS & T. SVITKINA

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Authors and Affiliations

  1. the MRC Laboratory for Molecular Cell Biology, Gower Street, WC1E 6BT, London, UK

    Laura M. Machesky

  2. the European Molecular Biology Laboratory, Meyerhofstrasse 1, D-69117, Heidelberg, Germany

    Michael Way

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  1. Laura M. Machesky
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  2. Michael Way
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Machesky, L., Way, M. Actin branches out. Nature 394, 125–126 (1998). https://doi.org/10.1038/28039

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