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Science 3 July 1998:
Vol. 281. no. 5373, pp. 105 - 108
DOI: 10.1126/science.281.5373.105
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Reports

Interaction of Human Arp2/3 Complex and the Listeria monocytogenes ActA Protein in Actin Filament Nucleation

Matthew D. Welch, * Jody Rosenblatt, Justin Skoble, Daniel A. Portnoy, Timothy J. Mitchison

Actin filament assembly at the cell surface of the pathogenic bacterium Listeria monocytogenes requires the bacterial ActA surface protein and the host cell Arp2/3 complex. Purified Arp2/3 complex accelerated the nucleation of actin polymerization in vitro, but pure ActA had no effect. However, when combined, the Arp2/3 complex and ActA synergistically stimulated the nucleation of actin filaments. This mechanism of activating the host Arp2/3 complex at the L. monocytogenes surface may be similar to the strategy used by cells to control Arp2/3 complex activity and hence the spatial and temporal distribution of actin polymerization.

M. D. Welch and J. Rosenblatt, Department of Cellular and Molecular Pharmacology, University of California, San Francisco, CA 94143, USA. T. J. Mitchison, Department of Cell Biology, Harvard Medical School, Boston, MA 02115, USA. J. Skoble and D. A. Portnoy, Department of Molecular and Cell Biology and School of Public Health, University of California, Berkeley, CA 94720, USA.
*   To whom correspondence should be addressed at Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720, USA.

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The Arp2/3 complex mediates actin polymerization induced by the small GTP-binding protein Cdc42.
L. Ma, R. Rohatgi, and M. W. Kirschner (1998)
PNAS 95, 15362-15367
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The Yeast V159N Actin Mutant Reveals Roles for Actin Dynamics In Vivo.
L. D. Belmont and D. G. Drubin (1998)
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Characterization of the Interaction between Zyxin and Members of the Ena/Vasodilator-stimulated Phosphoprotein Family of Proteins.
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Activation of the Arp2/3 Complex by the Listeria ActA Protein. ActA BINDS TWO ACTIN MONOMERS AND THREE SUBUNITS OF THE Arp2/3 COMPLEX.
J. Zalevsky, I. Grigorova, and R. D. Mullins (2001)
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Mechanisms of Cold-induced Platelet Actin Assembly.
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SCAR is a primary regulator of Arp2/3-dependent morphological events in Drosophila.
J. A. Zallen, Y. Cohen, A. M. Hudson, L. Cooley, E. Wieschaus, and E. D. Schejter (2002)
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