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

被引：410
作者：
Welch, MD
Rosenblatt, J
Skoble, J
Portnoy, DA
Mitchison, TJ
机构：
[1] Univ Calif Berkeley, Dept Mol & Cell Biol, Berkeley, CA 94720 USA
[2] Univ Calif San Francisco, Dept Mol & Cellular Pharmacol, San Francisco, CA 94143 USA
[3] Harvard Univ, Sch Med, Dept Cell Biol, Boston, MA 02115 USA
[4] Univ Calif Berkeley, Sch Publ Hlth, Berkeley, CA 94720 USA
来源：
SCIENCE | 1998年 / 281卷 / 5373期
关键词：
D O I：
10.1126/science.281.5373.105
中图分类号：
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号：
07 ; 0710 ; 09 ;
摘要：
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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页码：105 / 108
页数：4
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