Crystal Structure of Arp2/3 Complex

@article{Robinson2001CrystalSO,
  title={Crystal Structure of Arp2/3 Complex},
  author={Robert Charles Robinson and Kirsi Turbedsky and D A Kaiser and J B Marchand and Henry N. Higgs and Senyon Choe and Thomas D. 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… 
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X-ray scattering study of activated Arp2/3 complex with bound actin-WCA.

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References

SHOWING 1-10 OF 64 REFERENCES

Structure of Arp2/3 Complex in Its Activated State and in Actin Filament Branch Junctions

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.

Structure and function of the Arp2/3 complex.

The interaction of Arp2/3 complex with actin: nucleation, high affinity pointed end capping, and formation of branching networks of filaments.

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.

Activation of the yeast Arp2/3 complex by Bee1p, a WASP-family protein

The Human Arp2/3 Complex Is Composed of Evolutionarily Conserved Subunits and Is Localized to Cellular Regions of Dynamic Actin Filament Assembly

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.

Activation of the Arp2/3 Complex by the Listeria ActA Protein

This work shows that two domains of ActA with sequence similarity to WASP homology 2 domains bind two actin monomers with submicromolar affinity and proposes that ActA and endogenous WASP family proteins promote Arp 2/3-dependent nucleation by similar mechanisms and require simultaneous binding of Arp2 and Arp3.

The Interaction between N-WASP and the Arp2/3 Complex Links Cdc42-Dependent Signals to Actin Assembly

Structure, Subunit Topology, and Actin-binding Activity of the Arp2/3 Complex from Acanthamoeba

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.

The Arp2/3 complex nucleates actin filament branches from the sides of pre-existing filaments

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.

The Arp2/3 complex branches filament barbed ends: functional antagonism with capping proteins

It is shown that the activated Arp2/3 complex interacts with the barbed ends of filaments to initiate barbed-end branching, which quantitatively accounts for polymerization kinetics and for the length correlation of the branches offilaments observed by electron microscopy.
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