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.

引用

页码：105 / 108

页数：4

共 42 条

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