Crystal Structure of Arp2/3 Complex

@article{Robinson2001CrystalSO,
  title={Crystal Structure of Arp2/3 Complex},
  author={R. Robinson and K. Turbedsky and D. Kaiser and J. Marchand and H. Higgs and S. Choe and T. Pollard},
  journal={Science},
  year={2001},
  volume={294},
  pages={1679 - 1684}
}
We determined a crystal structure of bovine Arp2/3 complex, an assembly of seven proteins that initiates actin polymerization in eukaryotic cells, at 2.0 angstrom resolution. Actin-related protein 2 (Arp2) and Arp3 are folded like actin, with distinctive surface features. Subunits ARPC2 p34 and ARPC4 p20 in the core of the complex associate through long carboxyl-terminal α helices and have similarly folded amino-terminal α/β domains. ARPC1 p40 is a seven-blade β propeller with an insertion that… Expand
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TLDR
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TLDR
The seven-subunit Arp2/3 complex choreographs the formation of branched actin networks at the leading edge of migrating cells by initiating actin filament branches from the sides of existing filaments using asymmetric, oblate ellipsoids. Expand
Structure and function of the Arp2/3 complex.
TLDR
Chemical cross-linking implicates three subunits in binding the Arp2/3 complex to the side of another actin filament, and the Arps are thought to mediate pointed-end capping and nucleation. Expand
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TLDR
It is shown that the carboxy-terminal WA domain of WASP binds to a single actin monomer with a Kd of 0.6 μM in an equilibrium with rapid exchange rates, indicating that there may be an activation step in the nucleation pathway. Expand
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TLDR
It is shown that Arp2/3 complex purified from Acanthamoeba caps the pointed ends of actin filaments with high affinity and increases the critical concentration for polymerization at the pointed end from 0.6 to 1.0 microM. Expand
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TLDR
It is shown that Bee1p and the Arp2/3 complex co-immunoprecipitate when expressed at endogenous levels, and that this interaction requires both the Arc15p and Arc19p subunits of the ArP2/ 3 complex. Expand
The Human Arp2/3 Complex Is Composed of Evolutionarily Conserved Subunits and Is Localized to Cellular Regions of Dynamic Actin Filament Assembly
TLDR
The ability of the Arp2/3 complex to induce actin polymerization and its intracellular distribution suggest that the complex promotes actin assembly in lamellipodia and may participate in lameLLipodial protrusion. Expand
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TLDR
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The Interaction between N-WASP and the Arp2/3 Complex Links Cdc42-Dependent Signals to Actin Assembly
TLDR
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Structure, Subunit Topology, and Actin-binding Activity of the Arp2/3 Complex from Acanthamoeba
TLDR
Structural and topological models for the Arp2/3 complex are proposed and it is suggested that affinity for actin filaments accounts for the localization of complex subunits to actinrich regions of Acanthamoeba. Expand
The Arp2/3 complex nucleates actin filament branches from the sides of pre-existing filaments
TLDR
Results indicate that the activated Arp2/3 complex preferentially nucleates filament branches directly on the sides of pre-existing filaments, in contrast to the dendritic nucleation model for actin-network assembly. Expand
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