Spatial Control of Actin Filament Assembly Mary C Beckerle  Cell  Volume 95, Issue 6, Pages 741-748 (December 1998) DOI: 10.1016/S0092-8674(00)81697-9

Figure 1 Actin Assemblages (A) Actin-rich projections in the cochlea exhibit defined lengths and positions. (B) Semicrystalline actin arrays in striated muscle. (C) Zones of actin assembly (arrows) detected by incorporation of fluorescently labeled actin (red) at the leading edge of a migrating cell. (D) The actin-rich comet tails (arrows) of Listeria monocytogenes within host cytoplasm. Images shown here have been reproduced from the following sources: (A) Tilney et al., 1983, by copyright permission of the Rockefeller University Press; (B) Smith, 1972, by copyright permission of Academic Press, Inc.; (C) Chan et al., 1998 by copyright permission of the Company of Biologists, Ltd; (D) Alberts et al., 1994, courtesy of Tim Mitchison and Julie Theriot. Cell 1998 95, 741-748DOI: (10.1016/S0092-8674(00)81697-9)

Figure 2 Schematic Representation of the Listeria ActA Protein ActA displays a signal sequence, an N-terminal region that appears to interact with the Arp2/3 complex to nucleate actin assembly, a central series of proline-rich repeats that bind Ena/VASP proteins, and a C-terminal membrane anchor. No eukaryotic proteins with substantial similarity to the “nucleation” domain of ActA have been identified. In contrast, both vinculin and zyxin display sequences that are strikingly related to the “assembly-accelerating” domain of ActA. Although not depicted here, ActA is a dimer in vivo (Mourrain et al. 1997). Cell 1998 95, 741-748DOI: (10.1016/S0092-8674(00)81697-9)

Figure 3 Similarities between Actin Assembly on the Listeria Surface and at the Cytoplasmic Face of the Plasma Membrane A comparison of molecular models for actin assembly by Listeria within its eukaryotic host (top panel) and at the surface of an uninfected mammalian cell (bottom panel). The Listeria ActA protein appears to stimulate actin assembly by interacting with the Arp2/3 complex and members of the Ena/VASP family (E/V) that recruit profilin (P). In an uninfected mammalian cell, for example, Arp2/3 may be localized and activated at particular regions of the cell where actin assembly is to be favored. One region of the zyxin protein appears to function like ActA to recruit Ena/VASP and ultimately profilin. Zyxin also binds α-actinin, which could facilitate the cross-linking of newly assembled actin filaments as well as link zyxin directly to cell surface receptors such as integrins. When active, vav bound to zyxin may locally reduce actin filament capping, thus enhancing filament elongation. Cell adhesion to extracellular matrix can stimulate vectorial cell migration, but how is the adhesive event coupled to directional membrane protrusion? The diagram illustrates a potential mechanism for insuring the spatial coincidence of sites of substratum recognition by integrin receptors and the actin assembly machinery necessary for cell surface extension. Details are described in the text. Cell 1998 95, 741-748DOI: (10.1016/S0092-8674(00)81697-9)