Reconstitution of human Arp2/3 complex reveals critical roles of individual subunits in complex structure and activity

被引：140

作者：

Gournier, H ^{[1
]}

Goley, ED ^{[1
]}

Niederstrasser, H ^{[1
]}

Trinh, T ^{[1
]}

Welch, MD ^{[1
]}

机构：

[1] Univ Calif Berkeley, Dept Mol & Cell Biol, Berkeley, CA 94720 USA

来源：

MOLECULAR CELL | 2001年 / 8卷 / 05期

关键词：

D O I：

10.1016/S1097-2765(01)00393-8

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The Arp2/3 complex is a seven-protein assembly that is critical for actin nucleation and branching in cells. Here we report the reconstitution of active human Arp2/3 complex after expression of all seven subunits in insect cells. Expression of partial complexes revealed that a heterodimer of the p34 and p20 subunits constitutes a critical structural core of the complex, whereas the remaining subunits are peripherally located. Arp3 is crucial for nucleation, consistent with it being a structural component of the nucleation site. p41, p21, and p16 contribute differently to nucleation and stimulation by ActA and WASP, whereas p34/p20 bind actin filaments and likely function in actin branching. This study reveals that the nucleating and organizing functions of Arp2/3 complex subunits are separable, indicating that these activities may be differentially regulated in cells.

引用

页码：1041 / 1052

页数：12

共 41 条

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