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PDBsum entry 1k8k

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protein Protein-protein interface(s) links
Structural protein PDB id
1k8k
Jmol PyMol
Contents
Protein chains
401 a.a.
190 a.a. *
354 a.a. *
284 a.a. *
174 a.a. *
167 a.a. *
139 a.a. *
Waters ×1710
* Residue conservation analysis
PDB id:
1k8k
Name: Structural protein
Title: Crystal structure of arp2/3 complex
Structure: Actin-like protein 3. Chain: a. Synonym: arp3. Actin-related protein 3. Actin-2. Other_details: part of the arp2/3 complex. Actin-like protein 2. Chain: b. Synonym: arp2. Actin-related protein 2. Other_details: part of the arp2/3 complex. Arp2/3 complex 41 kda subunit.
Source: Bos taurus. Cattle. Organism_taxid: 9913. Organ: thymus. Organ: thymus
Biol. unit: Heptamer (from PQS)
Resolution:
2.00Å     R-factor:   0.216     R-free:   0.251
Authors: R.C.Robinson,K.Turbedsky,D.A.Kaiser,H.N.Higgs,J.-B.Marchand, S.Choe,T.D.Pollard
Key ref:
R.C.Robinson et al. (2001). Crystal structure of Arp2/3 complex. Science, 294, 1679-1684. PubMed id: 11721045 DOI: 10.1126/science.1066333
Date:
24-Oct-01     Release date:   07-Dec-01    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P61157  (ARP3_BOVIN) -  Actin-related protein 3
Seq:
Struc:
418 a.a.
401 a.a.
Protein chain
Pfam   ArchSchema ?
A7MB62  (ARP2_BOVIN) -  Actin-related protein 2
Seq:
Struc:
394 a.a.
190 a.a.
Protein chain
Pfam   ArchSchema ?
Q58CQ2  (ARC1B_BOVIN) -  Actin-related protein 2/3 complex subunit 1B
Seq:
Struc:
372 a.a.
354 a.a.*
Protein chain
Pfam   ArchSchema ?
Q3MHR7  (ARPC2_BOVIN) -  Actin-related protein 2/3 complex subunit 2
Seq:
Struc:
300 a.a.
284 a.a.
Protein chain
Pfam   ArchSchema ?
Q3T035  (ARPC3_BOVIN) -  Actin-related protein 2/3 complex subunit 3
Seq:
Struc:
178 a.a.
174 a.a.
Protein chain
Pfam   ArchSchema ?
Q148J6  (ARPC4_BOVIN) -  Actin-related protein 2/3 complex subunit 4
Seq:
Struc:
168 a.a.
167 a.a.
Protein chain
Pfam   ArchSchema ?
Q3SYX9  (ARPC5_BOVIN) -  Actin-related protein 2/3 complex subunit 5
Seq:
Struc:
151 a.a.
139 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 3 residue positions (black crosses)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     synapse   13 terms 
  Biological process     cell projection organization   7 terms 
  Biochemical function     nucleotide binding     8 terms  

 

 
DOI no: 10.1126/science.1066333 Science 294:1679-1684 (2001)
PubMed id: 11721045  
 
 
Crystal structure of Arp2/3 complex.
R.C.Robinson, K.Turbedsky, D.A.Kaiser, J.B.Marchand, H.N.Higgs, S.Choe, T.D.Pollard.
 
  ABSTRACT  
 
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 alpha helices and have similarly folded amino-terminal alpha/beta domains. ARPC1 p40 is a seven-blade beta propeller with an insertion that may associate with the side of an actin filament. ARPC3 p21 and ARPC5 p16 are globular alpha-helical subunits. We predict that WASp/Scar proteins activate Arp2/3 complex by bringing Arp2 into proximity with Arp3 for nucleation of a branch on the side of a preexisting actin filament.
 
  Selected figure(s)  
 
Figure 1.
Fig. 1. Atomic structure of bovine Arp2/3 complex viewed from the front. This standard view shows Arp2 in the classic actin orientation. (A) Stereopair of ribbon diagrams (40-42). Color codes for subunits: Arp3, orange; Arp2, red for subdomains 3 and 4, gray-red for the actin backbone model of subdomains 1 and 2; p40, green; p34, light blue; p20, dark blue; p21, magenta; p16, yellow. (B) Space-filling model with the subdomains of Arp2 and Arp3 indicated (43). (C) Space-filling model with the electrostatic potential indicated with blue as positive and red as negative (43). Both p21 and p40 have strongly basic surface patches. The actin backbone model of Arp2 subdomains 1 and 2 is outlined in (B) and (C).
Figure 2.
Fig. 2. Ribbon diagrams comparing actin and the two Arps in the Arp2/3 complex. (A) Rabbit skeletal muscle actin from the cocrystal with DNase I (PDB accession number 1ATN). (B) Arp2. Subdomains 3 and 4 are the refined model consisting of residues Gly154 to Arg343. The backbone of actin subdomains 1 and 2 (shaded gray-red) is positioned according to the experimental density of the helices in the refined map of the Arp2/3 complex. The insert Tyr325-Glu335 in subdomain 3 is colored green. (C) Arp3. The major inserts (Gln46 to Cys54, Thr154 to Arg161, Asn260 to Lys264, and Val347 to Leu358) are colored green. Residues 40 to 50 do not appear in the electron density map.
 
  The above figures are reprinted by permission from the AAAs: Science (2001, 294, 1679-1684) copyright 2001.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
21873984 B.Yu, H.C.Cheng, C.A.Brautigam, D.R.Tomchick, and M.K.Rosen (2011).
Mechanism of actin filament nucleation by the bacterial effector VopL.
  Nat Struct Mol Biol, 18, 1068-1074.
PDB code: 3seo
21993292 J.M.Kollman, A.Merdes, L.Mourey, and D.A.Agard (2011).
Microtubule nucleation by γ-tubulin complexes.
  Nat Rev Mol Cell Biol, 12, 709-721.  
21314430 R.Dominguez, and K.C.Holmes (2011).
Actin structure and function.
  Annu Rev Biophys, 40, 169-186.  
20538977 A.M.Ducka, P.Joel, G.M.Popowicz, K.M.Trybus, M.Schleicher, A.A.Noegel, R.Huber, T.A.Holak, and T.Sitar (2010).
Structures of actin-bound Wiskott-Aldrich syndrome protein homology 2 (WH2) domains of Spire and the implication for filament nucleation.
  Proc Natl Acad Sci U S A, 107, 11757-11762.
PDB codes: 3mmv 3mn5 3mn6 3mn7 3mn9
20133134 B.W.Bernstein, and J.R.Bamburg (2010).
ADF/cofilin: a functional node in cell biology.
  Trends Cell Biol, 20, 187-195.  
20404198 E.D.Goley, A.Rammohan, E.A.Znameroski, E.N.Firat-Karalar, D.Sept, and M.D.Welch (2010).
An actin-filament-binding interface on the Arp2/3 complex is critical for nucleation and branch stability.
  Proc Natl Acad Sci U S A, 107, 8159-8164.  
20071330 H.I.Balcer, K.Daugherty-Clarke, and B.L.Goode (2010).
The p40/ARPC1 subunit of Arp2/3 complex performs multiple essential roles in WASp-regulated actin nucleation.
  J Biol Chem, 285, 8481-8491.  
20833046 J.V.Small (2010).
Dicing with dogma: de-branching the lamellipodium.
  Trends Cell Biol, 20, 628-633.  
20207852 M.G.Roca, H.C.Kuo, A.Lichius, M.Freitag, and N.D.Read (2010).
Nuclear dynamics, mitosis, and the cytoskeleton during the early stages of colony initiation in Neurospora crassa.
  Eukaryot Cell, 9, 1171-1183.  
20446344 S.H.Lee, and R.Dominguez (2010).
Regulation of actin cytoskeleton dynamics in cells.
  Mol Cells, 29, 311-325.  
20657821 T.J.Jewett, N.J.Miller, C.A.Dooley, and T.Hackstadt (2010).
The conserved Tarp actin binding domain is important for chlamydial invasion.
  PLoS Pathog, 6, e1000997.  
19602153 A.I.Derman, E.C.Becker, B.D.Truong, A.Fujioka, T.M.Tucey, M.L.Erb, P.C.Patterson, and J.Pogliano (2009).
Phylogenetic analysis identifies many uncharacterized actin-like proteins (Alps) in bacteria: regulated polymerization, dynamic instability and treadmilling in Alp7A.
  Mol Microbiol, 73, 534-552.  
19648907 B.J.Nolen, N.Tomasevic, A.Russell, D.W.Pierce, Z.Jia, C.D.McCormick, J.Hartman, R.Sakowicz, and T.D.Pollard (2009).
Characterization of two classes of small molecule inhibitors of Arp2/3 complex.
  Nature, 460, 1031-1034.
PDB codes: 3dxk 3dxm
19217847 D.Van Valen, M.Haataja, and R.Phillips (2009).
Biochemistry on a leash: the roles of tether length and geometry in signal integration proteins.
  Biophys J, 96, 1275-1292.  
19129161 J.Maisch, J.Fiserová, L.Fischer, and P.Nick (2009).
Tobacco Arp3 is localized to actin-nucleating sites in vivo.
  J Exp Bot, 60, 603-614.  
19245710 N.Yutin, M.Y.Wolf, Y.I.Wolf, and E.V.Koonin (2009).
The origins of phagocytosis and eukaryogenesis.
  Biol Direct, 4, 9.  
19529941 P.Qian, S.Hou, and G.Guo (2009).
Molecular mechanisms controlling pavement cell shape in Arabidopsis leaves.
  Plant Cell Rep, 28, 1147-1157.  
19874150 R.Dominguez (2009).
Actin filament nucleation and elongation factors--structure-function relationships.
  Crit Rev Biochem Mol Biol, 44, 351-366.  
19176514 S.H.Soderling (2009).
Grab your partner with both hands: cytoskeletal remodeling by Arp2/3 signaling.
  Sci Signal, 2, pe5.  
19655310 S.K.Lee, Y.Kim, S.S.Kim, J.H.Lee, K.Cho, S.S.Lee, Z.W.Lee, K.H.Kwon, Y.H.Kim, H.Suh-Kim, J.S.Yoo, and Y.M.Park (2009).
Differential expression of cell surface proteins in human bone marrow mesenchymal stem cells cultured with or without basic fibroblast growth factor containing medium.
  Proteomics, 9, 4389-4405.  
20059951 S.M.Ferguson, S.Ferguson, A.Raimondi, S.Paradise, H.Shen, K.Mesaki, A.Ferguson, O.Destaing, G.Ko, J.Takasaki, O.Cremona, E.O' Toole, and P.De Camilli (2009).
Coordinated actions of actin and BAR proteins upstream of dynamin at endocytic clathrin-coated pits.
  Dev Cell, 17, 811-822.  
19012317 S.M.Pocha, and G.O.Cory (2009).
WAVE2 is regulated by multiple phosphorylation events within its VCA domain.
  Cell Motil Cytoskeleton, 66, 36-47.  
19158791 T.Oda, M.Iwasa, T.Aihara, Y.Maéda, and A.Narita (2009).
The nature of the globular- to fibrous-actin transition.
  Nature, 457, 441-445.
PDB code: 2zwh
  19382535 T.S.Wong, B.Brough, and C.M.Ho (2009).
Creation of functional micro/nano systems through top-down and bottom-up approaches.
  Mol Cell Biomech, 6, 1.  
19298826 W.D.Zencheck, H.Xiao, B.J.Nolen, R.H.Angeletti, T.D.Pollard, and S.C.Almo (2009).
Nucleotide- and activator-dependent structural and dynamic changes of arp2/3 complex monitored by hydrogen/deuterium exchange and mass spectrometry.
  J Mol Biol, 390, 414-427.  
19843465 Z.Zhang, J.Pfaendtner, A.Grafmüller, and G.A.Voth (2009).
Defining coarse-grained representations of large biomolecules and biomolecular complexes from elastic network models.
  Biophys J, 97, 2327-2337.  
18640983 B.J.Nolen, and T.D.Pollard (2008).
Structure and biochemical properties of fission yeast Arp2/3 complex lacking the Arp2 subunit.
  J Biol Chem, 283, 26490-26498.
PDB code: 3dwl
18509026 B.Rácz, and R.J.Weinberg (2008).
Organization of the Arp2/3 complex in hippocampal spines.
  J Neurosci, 28, 5654-5659.  
18703850 B.Stec, and K.A.Stieglitz (2008).
Not so clear on oxygen. Comment on Structural basis for cofactor-independent dioxygenation in vancomycin biosynthesis by Widboom et al. (2007), Nature (London), 447, 342-345.
  Acta Crystallogr D Biol Crystallogr, 64, 1000-1002.  
18316411 I.Rouiller, X.P.Xu, K.J.Amann, C.Egile, S.Nickell, D.Nicastro, R.Li, T.D.Pollard, N.Volkmann, and D.Hanein (2008).
The structural basis of actin filament branching by the Arp2/3 complex.
  J Cell Biol, 180, 887-895.  
17978090 J.M.Kollman, A.Zelter, E.G.Muller, B.Fox, L.M.Rice, T.N.Davis, and D.A.Agard (2008).
The Structure of the {gamma}-Tubulin Small Complex: Implications of Its Architecture and Flexibility for Microtubule Nucleation.
  Mol Biol Cell, 19, 207-215.  
18689676 K.Baek, X.Liu, F.Ferron, S.Shu, E.D.Korn, and R.Dominguez (2008).
Modulation of actin structure and function by phosphorylation of Tyr-53 and profilin binding.
  Proc Natl Acad Sci U S A, 105, 11748-11753.
PDB codes: 3chw 3ci5 3cip
18381280 K.M.Daugherty, and B.L.Goode (2008).
Functional surfaces on the p35/ARPC2 subunit of Arp2/3 complex required for cell growth, actin nucleation, and endocytosis.
  J Biol Chem, 283, 16950-16959.  
18316414 L.Cai, and J.E.Bear (2008).
Peering deeply inside the branch.
  J Cell Biol, 180, 853-855.  
18725535 L.L.LeClaire, M.Baumgartner, J.H.Iwasa, R.D.Mullins, and D.L.Barber (2008).
Phosphorylation of the Arp2/3 complex is necessary to nucleate actin filaments.
  J Cell Biol, 182, 647-654.  
18462674 M.Boczkowska, G.Rebowski, M.V.Petoukhov, D.B.Hayes, D.I.Svergun, and R.Dominguez (2008).
X-ray scattering study of activated Arp2/3 complex with bound actin-WCA.
  Structure, 16, 695-704.  
18577520 M.J.Footer, J.K.Lyo, and J.A.Theriot (2008).
Close packing of Listeria monocytogenes ActA, a natively unfolded protein, enhances F-actin assembly without dimerization.
  J Biol Chem, 283, 23852-23862.  
  19204818 N.V.Valeyev, A.K.Downing, J.Sondek, and C.Deane (2008).
Electrostatic and Functional Analysis of the Seven-Bladed WD beta-Propellers.
  Evol Bioinform Online, 4, 203-216.  
18462670 R.D.Mullins (2008).
Trapping fugitive filament formers.
  Structure, 16, 661-663.  
18644894 S.Nakao, A.Platek, S.Hirano, and M.Takeichi (2008).
Contact-dependent promotion of cell migration by the OL-protocadherin-Nap1 interaction.
  J Cell Biol, 182, 395-410.  
17942696 A.D.Liverman, H.C.Cheng, J.E.Trosky, D.W.Leung, M.L.Yarbrough, D.L.Burdette, M.K.Rosen, and K.Orth (2007).
Arp2/3-independent assembly of actin by Vibrio type III effector VopL.
  Proc Natl Acad Sci U S A, 104, 17117-17122.  
17499050 B.J.Nolen, and T.D.Pollard (2007).
Insights into the influence of nucleotides on actin family proteins from seven structures of Arp2/3 complex.
  Mol Cell, 26, 449-457.
PDB codes: 2p9i 2p9k 2p9l 2p9n 2p9p 2p9s 2p9u
17721515 B.Serrels, A.Serrels, V.G.Brunton, M.Holt, G.W.McLean, C.H.Gray, G.E.Jones, and M.C.Frame (2007).
Focal adhesion kinase controls actin assembly via a FERM-mediated interaction with the Arp2/3 complex.
  Nat Cell Biol, 9, 1046-1056.  
17123542 E.Di Luccio, B.Petschacher, J.Voegtli, H.T.Chou, H.Stahlberg, B.Nidetzky, and D.K.Wilson (2007).
Structural and kinetic studies of induced fit in xylulose kinase from Escherichia coli.
  J Mol Biol, 365, 783-798.
PDB codes: 2itm 2nlx
17251352 J.G.Kiselar, R.Mahaffy, T.D.Pollard, S.C.Almo, and M.R.Chance (2007).
Visualizing Arp2/3 complex activation mediated by binding of ATP and WASp using structural mass spectrometry.
  Proc Natl Acad Sci U S A, 104, 1552-1557.  
17394647 K.Hailesellasse Sene, C.J.Porter, G.Palidwor, C.Perez-Iratxeta, E.M.Muro, P.A.Campbell, M.A.Rudnicki, and M.A.Andrade-Navarro (2007).
Gene function in early mouse embryonic stem cell differentiation.
  BMC Genomics, 8, 85.  
17677942 N.J.Burroughs, and D.Marenduzzo (2007).
Nonequilibrium-driven motion in actin networks: comet tails and moving beads.
  Phys Rev Lett, 98, 238302.  
17956734 R.Ahuja, R.Pinyol, N.Reichenbach, L.Custer, J.Klingensmith, M.M.Kessels, and B.Qualmann (2007).
Cordon-bleu is an actin nucleation factor and controls neuronal morphology.
  Cell, 131, 337-350.  
17167782 R.Guo, H.Sakamoto, S.Sugiura, and M.Ogawa (2007).
Endothelial cell motility is compatible with junctional integrity.
  J Cell Physiol, 211, 327-335.  
17360432 R.Zoncu, R.M.Perera, R.Sebastian, F.Nakatsu, H.Chen, T.Balla, G.Ayala, D.Toomre, and P.V.De Camilli (2007).
Loss of endocytic clathrin-coated pits upon acute depletion of phosphatidylinositol 4,5-bisphosphate.
  Proc Natl Acad Sci U S A, 104, 3793-3798.  
17911258 S.H.Lee, D.B.Hayes, G.Rebowski, I.Tardieux, and R.Dominguez (2007).
Toxofilin from Toxoplasma gondii forms a ternary complex with an antiparallel actin dimer.
  Proc Natl Acad Sci U S A, 104, 16122-16127.
PDB code: 2q97
17477841 T.D.Pollard (2007).
Regulation of actin filament assembly by Arp2/3 complex and formins.
  Annu Rev Biophys Biomol Struct, 36, 451-477.  
16403731 A.E.Kelly, H.Kranitz, V.Dötsch, and R.D.Mullins (2006).
Actin binding to the central domain of WASP/Scar proteins plays a critical role in the activation of the Arp2/3 complex.
  J Biol Chem, 281, 10589-10597.  
17052456 A.Mylona, C.Fernández-Tornero, P.Legrand, M.Haupt, A.Sentenac, J.Acker, and C.W.Müller (2006).
Structure of the tau60/Delta tau91 subcomplex of yeast transcription factor IIIC: insights into preinitiation complex assembly.
  Mol Cell, 24, 221-232.
PDB code: 2j04
16407068 B.A.Appleton, P.Wu, and C.Wiesmann (2006).
The crystal structure of murine coronin-1: a regulator of actin cytoskeletal dynamics in lymphocytes.
  Structure, 14, 87-96.
PDB codes: 2aq5 2b4e
  16569237 D.L.Scott, G.Diez, and W.H.Goldmann (2006).
Protein-lipid interactions: correlation of a predictive algorithm for lipid-binding sites with three-dimensional structural data.
  Theor Biol Med Model, 3, 17.  
16880808 D.R.Kovar (2006).
Arp2/3 ATP hydrolysis: to branch or to debranch?
  Nat Cell Biol, 8, 783-785.  
16990851 E.D.Goley, and M.D.Welch (2006).
The ARP2/3 complex: an actin nucleator comes of age.
  Nat Rev Mol Cell Biol, 7, 713-726.  
16901698 E.Kerkhoff (2006).
Cellular functions of the Spir actin-nucleation factors.
  Trends Cell Biol, 16, 477-483.  
16826602 F.Carlsson, and E.J.Brown (2006).
Actin-based motility of intracellular bacteria, and polarized surface distribution of the bacterial effector molecules.
  J Cell Physiol, 209, 288-296.  
17010119 H.Schüler, and K.Matuschewski (2006).
Regulation of apicomplexan microfilament dynamics by a minimal set of actin-binding proteins.
  Traffic, 7, 1433-1439.  
16959963 J.B.Moseley, and B.L.Goode (2006).
The yeast actin cytoskeleton: from cellular function to biochemical mechanism.
  Microbiol Mol Biol Rev, 70, 605-645.  
16736254 J.Fiserová, K.Schwarzerová, J.Petrásek, and Z.Opatrný (2006).
ARP2 and ARP3 are localized to sites of actin filament nucleation in tobacco BY-2 cells.
  Protoplasma, 227, 119-128.  
16415925 J.M.Stevens, E.E.Galyov, and M.P.Stevens (2006).
Actin-dependent movement of bacterial pathogens.
  Nat Rev Microbiol, 4, 91.  
16606694 K.Krzewski, X.Chen, J.S.Orange, and J.L.Strominger (2006).
Formation of a WIP-, WASp-, actin-, and myosin IIA-containing multiprotein complex in activated NK cells and its alteration by KIR inhibitory signaling.
  J Cell Biol, 173, 121-132.  
16428279 T.J.Minehardt, P.A.Kollman, R.Cooke, and E.Pate (2006).
The open nucleotide pocket of the profilin/actin x-ray structure is unstable and closes in the absence of profilin.
  Biophys J, 90, 2445-2449.  
16459078 W.Chiu, M.L.Baker, and S.C.Almo (2006).
Structural biology of cellular machines.
  Trends Cell Biol, 16, 144-150.  
16641319 X.Wu, L.Zhu, J.Guo, D.Y.Zhang, and K.Lin (2006).
Prediction of yeast protein-protein interaction network: insights from the Gene Ontology and annotations.
  Nucleic Acids Res, 34, 2137-2150.  
15592479 A.A.Rodal, O.Sokolova, D.B.Robins, K.M.Daugherty, S.Hippenmeyer, H.Riezman, N.Grigorieff, and B.L.Goode (2005).
Conformational changes in the Arp2/3 complex leading to actin nucleation.
  Nat Struct Mol Biol, 12, 26-31.  
15657399 A.C.Martin, X.P.Xu, I.Rouiller, M.Kaksonen, Y.Sun, L.Belmont, N.Volkmann, D.Hanein, M.Welch, and D.G.Drubin (2005).
Effects of Arp2 and Arp3 nucleotide-binding pocket mutations on Arp2/3 complex function.
  J Cell Biol, 168, 315-328.  
15741975 A.H.Aguda, L.D.Burtnick, and R.C.Robinson (2005).
The state of the filament.
  EMBO Rep, 6, 220-226.  
16262445 C.Egile, I.Rouiller, X.P.Xu, N.Volkmann, R.Li, and D.Hanein (2005).
Mechanism of filament nucleation and branch stability revealed by the structure of the Arp2/3 complex at actin branch junctions.
  PLoS Biol, 3, e383.  
16275905 D.Chereau, F.Kerff, P.Graceffa, Z.Grabarek, K.Langsetmo, and R.Dominguez (2005).
Actin-bound structures of Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 and the implications for filament assembly.
  Proc Natl Acad Sci U S A, 102, 16644-16649.
PDB codes: 2a3z 2a40 2a41 2a42
16085776 E.Atilgan, D.Wirtz, and S.X.Sun (2005).
Morphology of the lamellipodium and organization of actin filaments at the leading edge of crawling cells.
  Biophys J, 89, 3589-3602.  
15694855 E.Gouin, M.D.Welch, and P.Cossart (2005).
Actin-based motility of intracellular pathogens.
  Curr Opin Microbiol, 8, 35-45.  
16183906 J.L.D'Agostino, and B.L.Goode (2005).
Dissection of Arp2/3 complex actin nucleation mechanism and distinct roles for its nucleation-promoting factors in Saccharomyces cerevisiae.
  Genetics, 171, 35-47.  
15770684 J.Mathur (2005).
The ARP2/3 complex: giving plant cells a leading edge.
  Bioessays, 27, 377-387.  
16195354 J.Muller, Y.Oma, L.Vallar, E.Friederich, O.Poch, and B.Winsor (2005).
Sequence and comparative genomic analysis of actin-related proteins.
  Mol Biol Cell, 16, 5736-5748.  
16341081 M.J.Deeks, and P.J.Hussey (2005).
Arp2/3 and SCAR: plants move to the fore.
  Nat Rev Mol Cell Biol, 6, 954-964.  
15817388 M.Selbach, and S.Backert (2005).
Cortactin: an Achilles' heel of the actin cytoskeleton targeted by pathogens.
  Trends Microbiol, 13, 181-189.  
16088870 R.Sunada, I.Görzer, Y.Oma, T.Yoshida, N.Suka, U.Wintersberger, and M.Harata (2005).
The nuclear actin-related protein Act3p/Arp4p is involved in the dynamics of chromatin-modulating complexes.
  Yeast, 22, 753-768.  
15975903 S.W.Clark, and M.D.Rose (2005).
Alanine scanning of Arp1 delineates a putative binding site for Jnm1/dynamitin and Nip100/p150Glued.
  Mol Biol Cell, 16, 3999-4012.  
14747342 A.E.Carlsson, M.A.Wear, and J.A.Cooper (2004).
End versus side branching by Arp2/3 complex.
  Biophys J, 86, 1074-1081.  
15070726 A.Gautreau, H.Y.Ho, J.Li, H.Steen, S.P.Gygi, and M.W.Kirschner (2004).
Purification and architecture of the ubiquitous Wave complex.
  Proc Natl Acad Sci U S A, 101, 4379-4383.  
15152089 A.Y.Madrona, and D.K.Wilson (2004).
The structure of Ski8p, a protein regulating mRNA degradation: Implications for WD protein structure.
  Protein Sci, 13, 1557-1565.
PDB code: 1sq9
15505213 B.J.Nolen, R.S.Littlefield, and T.D.Pollard (2004).
Crystal structures of actin-related protein 2/3 complex with bound ATP or ADP.
  Proc Natl Acad Sci U S A, 101, 15627-15632.
PDB codes: 1tyq 1u2v
15494313 E.D.Goley, S.E.Rodenbusch, A.C.Martin, and M.D.Welch (2004).
Critical conformational changes in the Arp2/3 complex are induced by nucleotide and nucleation promoting factor.
  Mol Cell, 16, 269-279.  
15329672 E.Irobi, A.H.Aguda, M.Larsson, C.Guerin, H.L.Yin, L.D.Burtnick, L.Blanchoin, and R.C.Robinson (2004).
Structural basis of actin sequestration by thymosin-beta4: implications for WH2 proteins.
  EMBO J, 23, 3599-3608.
PDB code: 1t44
15385624 J.Komano, K.Miyauchi, Z.Matsuda, and N.Yamamoto (2004).
Inhibiting the Arp2/3 complex limits infection of both intracellular mature vaccinia virus and primate lentiviruses.
  Mol Biol Cell, 15, 5197-5207.  
15630612 J.R.Sellers (2004).
Fifty years of contractility research post sliding filament hypothesis.
  J Muscle Res Cell Motil, 25, 475-482.  
15037301 L.A.Amos, F.van den Ent, and J.Löwe (2004).
Structural/functional homology between the bacterial and eukaryotic cytoskeletons.
  Curr Opin Cell Biol, 16, 24-31.  
15591790 L.F.Shyur, C.H.Chen, C.P.Lo, S.Y.Wang, P.L.Kang, S.J.Sun, C.A.Chang, C.M.Tzeng, and N.S.Yang (2004).
Induction of apoptosis in MCF-7 human breast cancer cells by phytochemicals from Anoectochilus formosanus.
  J Biomed Sci, 11, 928-939.  
15094799 M.J.Dayel, and R.D.Mullins (2004).
Activation of Arp2/3 complex: addition of the first subunit of the new filament by a WASP protein triggers rapid ATP hydrolysis on Arp2.
  PLoS Biol, 2, E91.  
15063870 M.K.Kandasamy, R.B.Deal, E.C.McKinney, and R.B.Meagher (2004).
Plant actin-related proteins.
  Trends Plant Sci, 9, 196-202.  
15169891 N.Martinez-Quiles, H.Y.Ho, M.W.Kirschner, N.Ramesh, and R.S.Geha (2004).
Erk/Src phosphorylation of cortactin acts as a switch on-switch off mechanism that controls its ability to activate N-WASP.
  Mol Cell Biol, 24, 5269-5280.  
15193311 R.B.Russell, F.Alber, P.Aloy, F.P.Davis, D.Korkin, M.Pichaud, M.Topf, and A.Sali (2004).
A structural perspective on protein-protein interactions.
  Curr Opin Struct Biol, 14, 313-324.  
14749719 R.K.Vadlamudi, F.Li, C.J.Barnes, R.Bagheri-Yarmand, and R.Kumar (2004).
p41-Arc subunit of human Arp2/3 complex is a p21-activated kinase-1-interacting substrate.
  EMBO Rep, 5, 154-160.  
15086808 S.El-Din El-Assal, J.Le, D.Basu, E.L.Mallery, and D.B.Szymanski (2004).
DISTORTED2 encodes an ARPC2 subunit of the putative Arabidopsis ARP2/3 complex.
  Plant J, 38, 526-538.  
  15499396 S.J.Clough, J.H.Tuteja, M.Li, L.F.Marek, R.C.Shoemaker, and L.O.Vodkin (2004).
Features of a 103-kb gene-rich region in soybean include an inverted perfect repeat cluster of CHS genes comprising the I locus.
  Genome, 47, 819-831.  
15697951 Y.Tseng, D.Wirtz, and D.Wirtz (2004).
Dendritic branching and homogenization of actin networks mediated by arp2/3 complex.
  Phys Rev Lett, 93, 258104.  
15006353 Y.Xu, J.B.Moseley, I.Sagot, F.Poy, D.Pellman, B.L.Goode, and M.J.Eck (2004).
Crystal structures of a Formin Homology-2 domain reveal a tethered dimer architecture.
  Cell, 116, 711-723.
PDB codes: 1ux4 1ux5
12547422 A.C.Gavin, and G.Superti-Furga (2003).
Protein complexes and proteome organization from yeast to man.
  Curr Opin Chem Biol, 7, 21-27.  
12857859 A.Gloss, F.Rivero, N.Khaire, R.Müller, W.F.Loomis, M.Schleicher, and A.A.Noegel (2003).
Villidin, a novel WD-repeat and villin-related protein from Dictyostelium, is associated with membranes and the cytoskeleton.
  Mol Biol Cell, 14, 2716-2727.  
12517700 A.M.Weaver, M.E.Young, W.L.Lee, and J.A.Cooper (2003).
Integration of signals to the Arp2/3 complex.
  Curr Opin Cell Biol, 15, 23-30.  
12743368 C.Le Clainche, D.Pantaloni, and M.F.Carlier (2003).
ATP hydrolysis on actin-related protein 2/3 complex causes debranching of dendritic actin arrays.
  Proc Natl Acad Sci U S A, 100, 6337-6342.  
12923524 E.H.Egelman (2003).
A tale of two polymers: new insights into helical filaments.
  Nat Rev Mol Cell Biol, 4, 621-630.  
12525261 G.D.Bader, and C.W.Hogue (2003).
An automated method for finding molecular complexes in large protein interaction networks.
  BMC Bioinformatics, 4, 2.  
12805231 H.Szerlong, A.Saha, and B.R.Cairns (2003).
The nuclear actin-related proteins Arp7 and Arp9: a dimeric module that cooperates with architectural proteins for chromatin remodeling.
  EMBO J, 22, 3175-3187.  
12906796 J.Le, S.e.l.-.D.El-Assal, D.Basu, M.E.Saad, and D.B.Szymanski (2003).
Requirements for Arabidopsis ATARP2 and ATARP3 during epidermal development.
  Curr Biol, 13, 1341-1347.  
14645530 K.Horie, K.Yusa, K.Yae, J.Odajima, S.E.Fischer, V.W.Keng, T.Hayakawa, S.Mizuno, G.Kondoh, T.Ijiri, Y.Matsuda, R.H.Plasterk, and J.Takeda (2003).
Characterization of Sleeping Beauty transposition and its application to genetic screening in mice.
  Mol Cell Biol, 23, 9189-9207.  
12655641 M.F.Carlier, C.Le Clainche, S.Wiesner, and D.Pantaloni (2003).
Actin-based motility: from molecules to movement.
  Bioessays, 25, 336-345.  
14611954 M.J.Deeks, and P.J.Hussey (2003).
Arp2/3 and 'the shape of things to come'.
  Curr Opin Plant Biol, 6, 561-567.  
12872157 S.C.Panchal, D.A.Kaiser, E.Torres, T.D.Pollard, and M.K.Rosen (2003).
A conserved amphipathic helix in WASP/Scar proteins is essential for activation of Arp2/3 complex.
  Nat Struct Biol, 10, 591-598.  
12578964 S.H.Soderling, L.K.Langeberg, J.A.Soderling, S.M.Davee, R.Simerly, J.Raber, and J.D.Scott (2003).
Loss of WAVE-1 causes sensorimotor retardation and reduced learning and memory in mice.
  Proc Natl Acad Sci U S A, 100, 1723-1728.  
12517699 S.J.Winder (2003).
Structural insights into actin-binding, branching and bundling proteins.
  Curr Opin Cell Biol, 15, 14-22.  
14621980 S.Ono (2003).
Regulation of actin filament dynamics by actin depolymerizing factor/cofilin and actin-interacting protein 1: new blades for twisted filaments.
  Biochemistry, 42, 13363-13370.  
12732734 S.Vorobiev, B.Strokopytov, D.G.Drubin, C.Frieden, S.Ono, J.Condeelis, P.A.Rubenstein, and S.C.Almo (2003).
The structure of nonvertebrate actin: implications for the ATP hydrolytic mechanism.
  Proc Natl Acad Sci U S A, 100, 5760-5765.
PDB codes: 1d4x 1nlv 1nm1 1nmd 1yag
12700767 T.D.Pollard (2003).
The cytoskeleton, cellular motility and the reductionist agenda.
  Nature, 422, 741-745.  
12600310 T.D.Pollard, and G.G.Borisy (2003).
Cellular motility driven by assembly and disassembly of actin filaments.
  Cell, 112, 453-465.  
12451597 T.H.Millard, B.Behrendt, S.Launay, K.Fütterer, and L.M.Machesky (2003).
Identification and characterisation of a novel human isoform of Arp2/3 complex subunit p16-ARC/ARPC5.
  Cell Motil Cytoskeleton, 54, 81-90.  
12350343 A.M.Edwards, B.Kus, R.Jansen, D.Greenbaum, J.Greenblatt, and M.Gerstein (2002).
Bridging structural biology and genomics: assessing protein interaction data with known complexes.
  Trends Genet, 18, 529-536.  
12429700 A.M.Hudson, and L.Cooley (2002).
Understanding the function of actin-binding proteins through genetic analysis of Drosophila oogenesis.
  Annu Rev Genet, 36, 455-488.  
12176354 A.M.Weaver, J.E.Heuser, A.V.Karginov, W.L.Lee, J.T.Parsons, and J.A.Cooper (2002).
Interaction of cortactin and N-WASp with Arp2/3 complex.
  Curr Biol, 12, 1270-1278.  
12499356 C.L.Humphries, H.I.Balcer, J.L.D'Agostino, B.Winsor, D.G.Drubin, G.Barnes, B.J.Andrews, and B.L.Goode (2002).
Direct regulation of Arp2/3 complex activity and function by the actin binding protein coronin.
  J Cell Biol, 159, 993.  
12194837 D.P.Kiehart, and J.D.Franke (2002).
Actin dynamics: the arp2/3 complex branches out.
  Curr Biol, 12, R557-R559.  
12366376 E.Giniger (2002).
How do Rho family GTPases direct axon growth and guidance? A proposal relating signaling pathways to growth cone mechanics.
  Differentiation, 70, 385-396.  
11839297 E.L.Borths, and M.D.Welch (2002).
Turning on the Arp2/3 complex at atomic resolution.
  Structure, 10, 131-135.  
12167670 E.P.Sablin, J.F.Dawson, M.S.VanLoock, J.A.Spudich, E.H.Egelman, and R.J.Fletterick (2002).
How does ATP hydrolysis control actin's associations?
  Proc Natl Acad Sci U S A, 99, 10945-10947.  
12486014 F.van den Ent, J.Møller-Jensen, L.A.Amos, K.Gerdes, and J.Löwe (2002).
F-actin-like filaments formed by plasmid segregation protein ParM.
  EMBO J, 21, 6935-6943.
PDB codes: 1mwk 1mwm
12464680 H.Falet, K.M.Hoffmeister, R.Neujahr, J.E.Italiano, T.P.Stossel, F.S.Southwick, and J.H.Hartwig (2002).
Importance of free actin filament barbed ends for Arp2/3 complex function in platelets and fibroblasts.
  Proc Natl Acad Sci U S A, 99, 16782-16787.  
12225681 H.N.Higgs (2002).
Actin nucleation: cortactin caught in the act.
  Curr Biol, 12, R593-R595.  
12473693 K.A.DeMali, C.A.Barlow, and K.Burridge (2002).
Recruitment of the Arp2/3 complex to vinculin: coupling membrane protrusion to matrix adhesion.
  J Cell Biol, 159, 881-891.  
12378539 L.S.Kaplow, A.d.e. .B.Chevance Ad, J.Henkel, and S.E.Malawista (2002).
Double-decker chemotaxis: no evidence for photonic stimulation of directed locomotion by human blood polymorphonuclear leukocytes.
  Cell Motil Cytoskeleton, 53, 289-292.  
12142282 M.A.Pufall, and B.J.Graves (2002).
Autoinhibitory domains: modular effectors of cellular regulation.
  Annu Rev Cell Dev Biol, 18, 421-462.  
12142287 M.D.Welch, and R.D.Mullins (2002).
Cellular control of actin nucleation.
  Annu Rev Cell Dev Biol, 18, 247-288.  
11835053 M.Kreishman-Deitrick, M.K.Rosen, and M.Kreishman-Deltrick (2002).
Ignition of a cellular machine.
  Nat Cell Biol, 4, E31-E33.  
11882539 M.R.Ahmadian, A.Wittinghofer, and G.Schmidt (2002).
The actin filament architecture: tightly regulated by the cells, manipulated by pathogens. International Titisee Conference on the actin cytoskeleton: from signalling to bacterial pathogenesis.
  EMBO Rep, 3, 214-218.  
12007413 V.Stevenson, A.Hudson, L.Cooley, and W.E.Theurkauf (2002).
Arp2/3-dependent pseudocleavage [correction of psuedocleavage] furrow assembly in syncytial Drosophila embryos.
  Curr Biol, 12, 705-711.  
11937049 Z.Jawad, and M.Paoli (2002).
Novel sequences propel familiar folds.
  Structure, 10, 447-454.  
11747805 J.A.Cooper, M.A.Wear, and A.M.Weaver (2001).
Arp2/3 complex: advances on the inner workings of a molecular machine.
  Cell, 107, 703-705.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.

 

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