T. D. Pollard and G. G. Borisy, Cellular motility driven by assembly and disassembly of actin filaments, Cell, vol.112, pp.453-465, 2003.
DOI : 10.1016/s0092-8674(03)00357-x
URL : https://doi.org/10.1016/s0092-8674(03)00357-x

M. Kaksonen, C. P. Toret, and D. G. Drubin, Harnessing actin dynamics for clathrin-mediated endocytosis, Nat Rev Mol Cell Biol, vol.7, pp.404-414, 2006.
DOI : 10.1038/nrm1940

J. D. Rotty, C. Wu, and J. E. Bear, New insights into the regulation and cellular functions of the ARP2/3 complex, Nat Rev Mol Cell Biol, vol.14, pp.7-12, 2013.

T. D. Pollard, Regulation of actin filament assembly by Arp2/3 complex and formins, Annu Rev Biophys Biomol Struct, vol.36, pp.451-477, 2007.
DOI : 10.1146/annurev.biophys.35.040405.101936

E. D. Goley and M. D. Welch, The ARP2/3 complex: an actin nucleator comes of age, Nat Rev Mol Cell Biol, vol.7, pp.713-726, 2006.

E. N. Firat-karalar and M. D. Welch, New mechanisms and functions of actin nucleation, Curr Opin Cell Biol, vol.23, pp.4-13, 2011.
DOI : 10.1016/j.ceb.2010.10.007
URL : http://europepmc.org/articles/pmc3073586?pdf=render

H. N. Higgs and T. D. Pollard, Regulation of actin filament network formation through ARP2/3 complex: activation by a diverse array of proteins, Annu Rev Biochem, vol.70, pp.649-676, 2001.

C. L. Humphries, H. I. Balcer, D. Agostino, J. L. Winsor, B. Drubin et al., Direct regulation of Arp2/3 complex activity and function by the actin binding protein coronin, J Cell Biol, vol.159, pp.993-1004, 2002.

L. Cai, A. M. Makhov, D. A. Schafer, and J. E. Bear, Coronin 1B antagonizes cortactin and remodels Arp2/3containing actin branches in lamellipodia, Cell, vol.134, pp.828-842, 2008.
DOI : 10.1016/j.cell.2008.06.054
URL : https://doi.org/10.1016/j.cell.2008.06.054

N. Foger, L. Rangell, D. M. Danilenko, and A. C. Chan, Requirement for coronin 1 in T lymphocyte trafficking and cellular homeostasis, Science, vol.313, pp.839-842, 2006.
DOI : 10.1126/science.1130563

S. L. Liu, K. M. Needham, J. R. May, and B. J. Nolen, Mechanism of a concentration-dependent switch between activation and inhibition of Arp2/3 complex by coronin, J Biol Chem, vol.286, pp.17039-17046, 2011.

M. Gandhi, B. A. Smith, M. Bovellan, V. Paavilainen, K. Daugherty-clarke et al., GMF is a cofilin homolog that binds Arp2/3 complex to stimulate filament debranching and inhibit actin nucleation, Curr Biol, vol.20, pp.861-867, 2010.
DOI : 10.1016/j.cub.2010.03.026
URL : https://doi.org/10.1016/j.cub.2010.03.026

C. A. Ydenberg, S. B. Padrick, M. O. Sweeney, M. Gandhi, O. Sokolova et al., GMF severs actinArp2/3 complex branch junctions by a cofilin-like mechanism, Curr Biol, vol.23, pp.1037-1045, 2013.
DOI : 10.1016/j.cub.2013.04.058
URL : https://doi.org/10.1016/j.cub.2013.04.058

Q. Luan and B. J. Nolen, Structural basis for regulation of Arp2/3 complex by GMF, Nat Struct Mol Biol, vol.20, pp.1062-1068, 2013.
DOI : 10.1038/nsmb.2628
URL : http://europepmc.org/articles/pmc3766443?pdf=render

T. Maritzen, T. Zech, M. R. Schmidt, E. Krause, L. M. Machesky et al., Gadkin negatively regulates cell spreading and motility via sequestration of the actin-nucleating ARP2/3 complex, Proc Natl Acad Sci U S A, vol.109, pp.10382-10387, 2012.

I. Dang, R. Gorelik, C. Sousa-blin, E. Derivery, C. Guerin et al., Inhibitory signalling to the Arp2/3 complex steers cell migration, Nature, vol.503, pp.281-284, 2013.
DOI : 10.1038/nature12611
URL : https://hal.archives-ouvertes.fr/hal-00920076

N. Volkmann, K. J. Amann, S. Stoilova-mcphie, C. Egile, D. C. Winter et al., Structure of Arp2/3 complex in its activated state and in actin filament branch junctions, Science, vol.293, pp.2456-2459, 2001.

C. Egile, I. Rouiller, X. P. Xu, N. Volkmann, R. Li et al., Mechanism of filament nucleation and branch stability revealed by the structure of the Arp2/3 complex at actin branch junctions, PLoS Biol, vol.3, p.383, 2005.

I. Rouiller, X. P. Xu, K. J. Amann, C. Egile, S. Nickell et al., The structural basis of actin filament branching by the Arp2/3 complex, J Cell Biol, vol.180, pp.887-895, 2008.

X. P. Xu, I. Rouiller, B. D. Slaughter, C. Egile, E. Kim et al., Three-dimensional reconstructions of Arp2/3 complex with bound nucleation promoting factors, Embo J, vol.31, pp.236-247, 2012.
DOI : 10.1038/emboj.2011.343
URL : http://emboj.embopress.org/content/31/1/236.full.pdf

A. A. Rodal, O. Sokolova, D. B. Robins, K. M. Daugherty, S. Hippenmeyer et al., Conformational changes in the Arp2/3 complex leading to actin nucleation, Nat Struct Mol Biol, vol.12, pp.26-31, 2005.
DOI : 10.1038/nsmb870

A. C. Martin, X. P. Xu, I. Rouiller, M. Kaksonen, Y. Sun et al., Effects of Arp2 and Arp3 nucleotide-binding pocket mutations on Arp2/3 complex function, J Cell Biol, vol.168, pp.315-328, 2005.
DOI : 10.1083/jcb.200408177
URL : http://jcb.rupress.org/content/jcb/168/2/315.full.pdf

R. D. Mullins, J. A. Heuser, and T. D. Pollard, The interaction of Arp2/3 complex with actin: nucleation, high affinity pointed end capping, and formation of branching networks of filaments, Proc Natl Acad Sci U S A, vol.95, pp.6181-6186, 1998.

L. Blanchoin, K. J. Amann, H. N. Higgs, J. B. Marchand, D. A. Kaiser et al., Direct observation of dendritic actin filament networks nucleated by Arp2/3 complex and WASP/Scar proteins, Nature, vol.404, pp.1007-1011, 2000.
DOI : 10.1038/35010008

K. J. Amann and T. D. Pollard, The Arp2/3 complex nucleates actin filament branches from the sides of pre-existing filaments, Nat Cell Biol, vol.3, pp.306-310, 2001.

B. A. Smith, S. B. Padrick, L. K. Doolittle, K. Daugherty-clarke, I. R. Correa et al., Three-color single molecule imaging shows WASP detachment from Arp2/3 complex triggers actin filament branch formation, Elife, vol.2, 2013.
DOI : 10.7554/elife.01008
URL : https://doi.org/10.7554/elife.01008

B. A. Smith, J. Gelles, and B. L. Goode, Single-molecule studies of actin assembly and disassembly factors, Methods Enzymol, vol.540, pp.95-117, 2014.
DOI : 10.1016/b978-0-12-397924-7.00006-6
URL : http://europepmc.org/articles/pmc4037564?pdf=render

M. Boczkowska, G. Rebowski, D. J. Kast, and R. Dominguez, Structural analysis of the transitional state of Arp2/3 complex activation by two actin-bound WCAs, Nature communications, vol.5, p.3308, 2014.

S. B. Padrick, L. K. Doolittle, C. A. Brautigam, D. S. King, and M. K. Rosen, Arp2/3 complex is bound and activated by two WASP proteins, Proceedings of the National Academy of Sciences of the United States of America, vol.108, pp.472-479, 2011.
DOI : 10.1073/pnas.1100236108
URL : http://www.pnas.org/content/108/33/E472.full.pdf

S. C. Ti, C. T. Jurgenson, B. J. Nolen, and T. D. Pollard, Structural and biochemical characterization of two binding sites for nucleation-promoting factor WASp-VCA on Arp2/3 complex, Proceedings of the National Academy of Sciences of the United States of America, vol.108, pp.463-471, 2011.

A. K. Goroncy, S. Koshiba, N. Tochio, T. Tomizawa, M. Sato et al., NMR solution structures of actin depolymerizing factor homology domains, Protein Sci, vol.18, pp.2384-2392, 2009.

M. Poukkula, M. Hakala, N. Pentinmikko, M. O. Sweeney, S. Jansen et al., GMF promotes leading-edge dynamics and collective cell migration in vivo, Curr Biol, vol.24, pp.2533-2540, 2014.

E. M. Haynes, S. B. Asokan, S. J. King, H. E. Johnson, J. M. Haugh et al., GMFbeta controls branched actin content and lamellipodial retraction in fibroblasts, J Cell Biol, vol.209, pp.803-812, 2015.

B. L. Goode, J. J. Wong, A. C. Butty, M. Peter, A. L. Mccormack et al., Coronin promotes the rapid assembly and cross-linking of actin filaments and may link the actin and microtubule cytoskeletons in yeast, The Journal of cell biology, vol.144, pp.83-98, 1999.

Z. Spoerl, M. Stumpf, A. A. Noegel, and A. Hasse, Oligomerization, F-actin interaction, and membrane association of the ubiquitous mammalian coronin 3 are mediated by its carboxyl terminus, J Biol Chem, vol.277, pp.48858-48867, 2002.

J. Gatfield, A. I. Zanolari, B. Steinmetz, M. O. Pieters, and J. , Association of the leukocyte plasma membrane with the actin cytoskeleton through coiled coil-mediated trimeric coronin 1 molecules, Mol Biol Cell, vol.16, pp.2786-2798, 2005.

E. D. Goley, A. Rammohan, E. A. Znameroski, E. N. Firat-karalar, D. Sept et al., An actinfilament-binding interface on the Arp2/3 complex is critical for nucleation and branch stability, Proc Natl Acad Sci U S A, vol.107, pp.8159-8164, 2010.

A. A. Rodal, A. L. Manning, B. L. Goode, and D. G. Drubin, Negative regulation of yeast WASp by two SH3 domain-containing proteins, Curr Biol, vol.13, pp.1000-1008, 2003.

Y. Sun, A. C. Martin, and D. G. Drubin, Endocytic internalization in budding yeast requires coordinated actin nucleation and myosin motor activity, Dev Cell, vol.11, pp.33-46, 2006.

S. Fetics, A. Thureau, V. Campanacci, M. Aumont-nicaise, I. Dang et al., Hybrid Structural Analysis of the Arp2/3 Regulator Arpin Identifies Its Acidic Tail as a Primary Binding Epitope, Structure, vol.24, pp.252-260, 2016.

E. D. Goley, S. E. Rodenbusch, A. C. Martin, and M. D. Welch, Critical conformational changes in the Arp2/3 complex are induced by nucleotide and nucleation promoting factor, Molecular cell, vol.16, pp.269-279, 2004.

S. B. Padrick and M. K. Rosen, Physical mechanisms of signal integration by WASP family proteins, Annu Rev Biochem, vol.79, pp.707-735, 2010.

L. Cai and J. E. Bear, Peering deeply inside the branch, J Cell Biol, vol.180, pp.853-855, 2008.

P. Dalhaimer and T. D. Pollard, Molecular dynamics simulations of Arp2/3 complex activation, Biophys J, vol.99, pp.2568-2576, 2010.

J. Pfaendtner and G. A. Voth, Molecular dynamics simulation and coarse-grained analysis of the Arp2/3 complex, Biophys J, vol.95, pp.5324-5333, 2008.

M. Gandhi, V. Achard, L. Blanchoin, and B. L. Goode, Coronin switches roles in actin disassembly depending on the nucleotide state of actin, Mol Cell, vol.34, pp.364-374, 2009.
URL : https://hal.archives-ouvertes.fr/hal-00398334

C. A. Ydenberg, B. A. Smith, D. Breitsprecher, J. Gelles, and B. L. Goode, Cease-fire at the leading edge: new perspectives on actin filament branching, debranching, and cross-linking, Cytoskeleton, vol.68, pp.596-602, 2011.

S. J. Ludtke, P. R. Baldwin, W. Chiu, and . Eman, Semiautomated software for high-resolution singleparticle reconstructions, J Struct Biol, vol.128, pp.82-97, 1999.

M. Van-heel, G. Harauz, E. V. Orlova, R. Schmidt, and M. Schatz, A new generation of the IMAGIC image processing system, J Struct Biol, vol.116, pp.17-24, 1996.

N. Grigorieff, FREALIGN: high-resolution refinement of single particle structures, J Struct Biol, vol.157, pp.117-125, 2007.
DOI : 10.1016/j.jsb.2006.05.004

T. D. Goddard, C. C. Huang, and T. E. Ferrin, Visualizing density maps with UCSF Chimera, J Struct Biol, vol.157, pp.281-287, 2007.
DOI : 10.1016/j.jsb.2006.06.010