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

Article Details

Citation

Gournier H, Goley ED, Niederstrasser H, Trinh T, Welch MD

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

Mol Cell. 2001 Nov;8(5):1041-52.

PubMed ID
11741539 [ View in PubMed
]
Abstract

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.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Actin-related protein 2/3 complex subunit 1BO15143Details
Actin-related protein 2P61160Details
Actin-related protein 3P61158Details
Actin-related protein 2/3 complex subunit 2O15144Details
Actin-related protein 2/3 complex subunit 3O15145Details
Actin-related protein 2/3 complex subunit 4P59998Details
Actin-related protein 2/3 complex subunit 5O15511Details