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. 1998 Jul 3;281(5373):105-8.
doi: 10.1126/science.281.5373.105.

Interaction of human Arp2/3 complex and the Listeria monocytogenes ActA protein in actin filament nucleation

M D Welch  1 , J Rosenblatt, J Skoble, D A Portnoy, T J Mitchison
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Interaction of human Arp2/3 complex and the Listeria monocytogenes ActA protein in actin filament nucleation

M D Welch et al. Science. .

Abstract

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.

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