| Literature DB >> 9651243 |
M D Welch1, J Rosenblatt, J Skoble, D A Portnoy, T J Mitchison.
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.Entities:
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Year: 1998 PMID： 9651243 DOI： 10.1126/science.281.5373.105
Source DB: PubMed Journal: Science ISSN： 0036-8075 Impact factor: 47.728