{"fulldoi":"https://doi.org/10.1038/nsmb870","volume":12,"article_processing_charge":"No","_id":"3141","external_id":{"pmid":["15592479"]},"year":"2004","user_id":"317138e5-6ab7-11ef-aa6d-ffef3953e345","extern":"1","author":[{"last_name":"Rodal","full_name":"Rodal, Avital","first_name":"Avital"},{"first_name":"Olga","full_name":"Sokolova, Olga","last_name":"Sokolova"},{"last_name":"Robins","full_name":"Robins, Deborah","first_name":"Deborah"},{"last_name":"Daugherty","full_name":"Daugherty, Karen","first_name":"Karen"},{"last_name":"Hippenmeyer","full_name":"Hippenmeyer, Simon","first_name":"Simon","id":"37B36620-F248-11E8-B48F-1D18A9856A87","orcid":"0000-0003-2279-1061"},{"first_name":"Howard","full_name":"Riezman, Howard","last_name":"Riezman"},{"first_name":"Nikolaus","full_name":"Grigorieff, Nikolaus","last_name":"Grigorieff"},{"first_name":"Bruce","last_name":"Goode","full_name":"Goode, Bruce"}],"article_type":"original","abstract":[{"lang":"eng","text":"The two actin-related subunits of the Arp2/3 complex, Arp2 and Arp3, are proposed to form a pseudo actin dimer that nucleates actin polymerization. However, in the crystal structure of the inactive complex, they are too far apart to form such a nucleus. Here, we show using EM that yeast and bovine Arp2/3 complexes exist in a distribution among open, intermediate and closed conformations. The crystal structure docks well into the open conformation. The activator WASp binds at the cleft between Arp2 and Arp3, and all WASp-bound complexes are closed. The inhibitor coronin binds near the p35 subunit, and all coronin-bound complexes are open. Activating and loss-of-function mutations in the p35 subunit skew conformational distribution in opposite directions, closed and open, respectively. We conclude that WASp stabilizes p35-dependent closure of the complex, holding Arp2 and Arp3 closer together to nucleate an actin filament."}],"publication":"Nature Structural and Molecular Biology","pmid":1,"publication_status":"published","das_tickbox":"1","date_published":"2004-12-12T00:00:00Z","OA_type":"closed access","date_updated":"2026-07-15T12:44:10Z","issue":"1","status":"public","publist_id":"3554","publisher":"Nature Publishing Group","citation":{"short":"A. Rodal, O. Sokolova, D. Robins, K. Daugherty, S. Hippenmeyer, H. Riezman, N. Grigorieff, B. Goode, Nature Structural and Molecular Biology 12 (2004) 26–31.","ieee":"A. Rodal et al., “Conformational changes in the Arp2 3 complex leading to actin nucleation,” Nature Structural and Molecular Biology, vol. 12, no. 1. Nature Publishing Group, pp. 26–31, 2004.","mla":"Rodal, Avital, et al. “Conformational Changes in the Arp2 3 Complex Leading to Actin Nucleation.” Nature Structural and Molecular Biology, vol. 12, no. 1, Nature Publishing Group, 2004, pp. 26–31, doi:10.1038/nsmb870.","ista":"Rodal A, Sokolova O, Robins D, Daugherty K, Hippenmeyer S, Riezman H, Grigorieff N, Goode B. 2004. Conformational changes in the Arp2 3 complex leading to actin nucleation. Nature Structural and Molecular Biology. 12(1), 26–31.","apa":"Rodal, A., Sokolova, O., Robins, D., Daugherty, K., Hippenmeyer, S., Riezman, H., … Goode, B. (2004). Conformational changes in the Arp2 3 complex leading to actin nucleation. Nature Structural and Molecular Biology. Nature Publishing Group. https://doi.org/10.1038/nsmb870","chicago":"Rodal, Avital, Olga Sokolova, Deborah Robins, Karen Daugherty, Simon Hippenmeyer, Howard Riezman, Nikolaus Grigorieff, and Bruce Goode. “Conformational Changes in the Arp2 3 Complex Leading to Actin Nucleation.” Nature Structural and Molecular Biology. Nature Publishing Group, 2004. https://doi.org/10.1038/nsmb870.","ama":"Rodal A, Sokolova O, Robins D, et al. Conformational changes in the Arp2 3 complex leading to actin nucleation. Nature Structural and Molecular Biology. 2004;12(1):26-31. doi:10.1038/nsmb870"},"intvolume":" 12","month":"12","publication_identifier":{"eissn":["1545-9985"],"issn":["1545-9993"]},"day":"12","title":"Conformational changes in the Arp2 3 complex leading to actin nucleation","page":"26 - 31","oa_version":"None","date_created":"2018-12-11T12:01:38Z","type":"journal_article","language":[{"iso":"eng"}],"doi":"10.1038/nsmb870"}