Reconstitution of human Arp2/3 complex reveals critical roles of individual subunits in complex structure and activity.
Article Details
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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
Name UniProt ID Actin-related protein 2/3 complex subunit 1B O15143 Details Actin-related protein 2 P61160 Details Actin-related protein 3 P61158 Details Actin-related protein 2/3 complex subunit 2 O15144 Details Actin-related protein 2/3 complex subunit 3 O15145 Details Actin-related protein 2/3 complex subunit 4 P59998 Details Actin-related protein 2/3 complex subunit 5 O15511 Details