Journal
MOLECULAR CELL
Volume 8, Issue 5, Pages 1041-1052Publisher
CELL PRESS
DOI: 10.1016/S1097-2765(01)00393-8
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Funding
- NIGMS NIH HHS [GM59609, R01 GM059609-03, R01 GM059609] Funding Source: Medline
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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.
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