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
View on AAAS
ncbi.nlm.nih.gov
489 Citations
Highly Influential Citations
25
Background Citations
216
Methods Citations
24
Results Citations
4

489 Citations

Citation Type

Citation Type

Insights into the influence of nucleotides on actin family proteins from seven structures of Arp2/3 complex.
ATP is required for nucleation of actin filament branches by Arp2/3 complex, but the influence of ATP binding and hydrolysis are poorly understood. We determined crystal structures of bovine Arp2/3… Expand
Conformational changes in the Arp2/3 complex leading to actin nucleation
TLDR
It is shown using EM that yeast and bovine Arp2/3 complexes exist in a distribution among open, intermediate and closed conformations, and it is concluded that WASp stabilizes p35-dependent closure of the complex, holding Arp 2 and Arp3 closer together to nucleate an actin filament. Expand
Structure and Biochemical Properties of Fission Yeast Arp2/3 Complex Lacking the Arp2 Subunit*
TLDR
The role of the Arp2 subunit in the function of Arp 2/3 complex is addressed by isolating a version of the complex lacking ArP2 (Arp2Δ Arp3/3complex) from fission yeast and finding that Arp1 does not contribute to the affinity of thecomplex for Wsp1-VCA, a Schizosaccharomyces pombe nucleation-promoting factor protein. Expand
Structure of the full-length yeast Arp7-Arp9 heterodimer.
TLDR
The Arp7-Arp9 structure reveals that its dimerization interface is not altered when bound in a complex with the SWI/SNF Snf2 HSA domain and the regulatory protein Rtt102, and is unlikely to form an actin-like filament based on modelling using the structure. Expand
Crystal structures of actin-related protein 2/3 complex with bound ATP or ADP.
Actin-related protein (Arp) 2/3 complex stimulates formation of actin filaments at the leading edge of motile cells. Nucleation of filaments depends on hydrolysis of ATP bound to Arp2. Here we report… Expand
X-ray scattering study of activated Arp2/3 complex with bound actin-WCA.
TLDR
A stable activated complex is engineered consisting of Arp2/3 complex, the WCA activator region of N-WASP, and one actin monomer, and studied its structure in solution by small angle X-ray scattering (SAXS). Expand
Molecular dynamics simulations of Arp2/3 complex activation.
TLDR
This work used atomistic-scale molecular dynamics simulations to drive Arp2 toward the position observed in branch junctions, and found that the active structure buried more surface area than the inactive conformation. Expand
The structural basis of actin filament branching by the Arp2/3 complex
The actin-related protein 2/3 (Arp2/3) complex mediates the formation of branched actin filaments at the leading edge of motile cells and in the comet tails moving certain intracellular pathogens.… Expand
Arp2/3 complex is bound and activated by two WASP proteins
TLDR
It is shown that activation most likely involves engagement of two distinct sites on Arp2/3 complex by two VCA molecules, each delivering an actin monomer. Expand
Cryo-EM structure of NPF-bound human Arp2/3 complex and activation mechanism
TLDR
Cryo-EM structure and functional study show that Arp2/3 complex activation requires NPF-mediated delivery of actin to both Arps, and structure-guided mutagenesis of theNPF-binding sites reveals their distinct roles in activation. Expand
...
1
2
3
4
5
...

References

SHOWING 1-10 OF 67 REFERENCES
Structure of Arp2/3 Complex in Its Activated State and in Actin Filament Branch Junctions
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
Interaction of WASP/Scar proteins with actin and vertebrate Arp2/3 complex
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
The interaction of Arp2/3 complex with actin: nucleation, high affinity pointed end capping, and formation of branching networks of filaments.
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
Activation of the yeast Arp2/3 complex by Bee1p, a WASP-family protein
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
Activation of the Arp2/3 Complex by the Listeria ActA Protein
TLDR
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. Expand
The Interaction between N-WASP and the Arp2/3 Complex Links Cdc42-Dependent Signals to Actin Assembly
TLDR
N-WASP and the Arp2/3 complex comprise a core mechanism that directly connects signal transduction pathways to the stimulation of actin polymerization. Expand
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
...
1
2
3
4
5
...