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…
509 Citations
Insights into the influence of nucleotides on actin family proteins from seven structures of Arp2/3 complex.
- ChemistryMolecular cell
- 2007
Conformational changes in the Arp2/3 complex leading to actin nucleation
- ChemistryNature Structural &Molecular Biology
- 2005
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.
Structure and Biochemical Properties of Fission Yeast Arp2/3 Complex Lacking the Arp2 Subunit*
- BiologyJournal of Biological Chemistry
- 2008
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.
Structure of the full-length yeast Arp7-Arp9 heterodimer.
- ChemistryActa crystallographica. Section D, Biological crystallography
- 2014
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.
Crystal structures of actin-related protein 2/3 complex with bound ATP or ADP.
- ChemistryProceedings of the National Academy of Sciences of the United States of America
- 2004
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…
Structure of Arp2/3 complex at a branched actin filament junction resolved by single-particle cryo-electron microscopy
- Biology, ChemistryProceedings of the National Academy of Sciences of the United States of America
- 2022
This work determined a high-resolution structure of the WasP-activated Arp2/3 complex at a branch junction and used biochemical, cell biological, and molecular dynamic simulations to understand the mechanism of WASP-mediated activation.
X-ray scattering study of activated Arp2/3 complex with bound actin-WCA.
- ChemistryStructure
- 2008
The structural basis of actin filament branching by the Arp2/3 complex
- ChemistryThe Journal of cell biology
- 2008
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.…
Arp2/3 complex is bound and activated by two WASP proteins
- Biology, ChemistryProceedings of the National Academy of Sciences
- 2011
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.
Cryo-EM structure of NPF-bound human Arp2/3 complex and activation mechanism
- Biology, ChemistryScience Advances
- 2020
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.
References
SHOWING 1-10 OF 64 REFERENCES
Structure of Arp2/3 Complex in Its Activated State and in Actin Filament Branch Junctions
- BiologyScience
- 2001
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.
The interaction of Arp2/3 complex with actin: nucleation, high affinity pointed end capping, and formation of branching networks of filaments.
- BiologyProceedings of the National Academy of Sciences of the United States of America
- 1998
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
- BiologyCurrent Biology
- 1999
The Human Arp2/3 Complex Is Composed of Evolutionarily Conserved Subunits and Is Localized to Cellular Regions of Dynamic Actin Filament Assembly
- BiologyThe Journal of cell biology
- 1997
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
- Biology, ChemistryThe Journal of Biological Chemistry
- 2001
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
- BiologyCell
- 1999
Structure, Subunit Topology, and Actin-binding Activity of the Arp2/3 Complex from Acanthamoeba
- BiologyThe Journal of cell biology
- 1997
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
- BiologyNature Cell Biology
- 2001
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
- BiologyNature Cell Biology
- 2000
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.