{"OA_type":"closed access","type":"journal_article","oa_version":"None","extern":"1","publication_status":"published","doi":"10.1038/nsmb870","year":"2004","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.","mla":"Rodal, Avital, et al. “Conformational Changes in the Arp2 3 Complex Leading to Actin Nucleation.” <i>Nature Structural and Molecular Biology</i>, vol. 12, no. 1, Nature Publishing Group, 2004, pp. 26–31, doi:<a href=\"https://doi.org/10.1038/nsmb870\">10.1038/nsmb870</a>.","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.” <i>Nature Structural and Molecular Biology</i>. Nature Publishing Group, 2004. <a href=\"https://doi.org/10.1038/nsmb870\">https://doi.org/10.1038/nsmb870</a>.","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. <i>Nature Structural and Molecular Biology</i>. Nature Publishing Group. <a href=\"https://doi.org/10.1038/nsmb870\">https://doi.org/10.1038/nsmb870</a>","ama":"Rodal A, Sokolova O, Robins D, et al. Conformational changes in the Arp2 3 complex leading to actin nucleation. <i>Nature Structural and Molecular Biology</i>. 2004;12(1):26-31. doi:<a href=\"https://doi.org/10.1038/nsmb870\">10.1038/nsmb870</a>","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.","ieee":"A. Rodal <i>et al.</i>, “Conformational changes in the Arp2 3 complex leading to actin nucleation,” <i>Nature Structural and Molecular Biology</i>, vol. 12, no. 1. Nature Publishing Group, pp. 26–31, 2004."},"volume":12,"page":"26 - 31","issue":"1","author":[{"first_name":"Avital","last_name":"Rodal","full_name":"Rodal, Avital"},{"full_name":"Sokolova, Olga","first_name":"Olga","last_name":"Sokolova"},{"first_name":"Deborah","last_name":"Robins","full_name":"Robins, Deborah"},{"full_name":"Daugherty, Karen","last_name":"Daugherty","first_name":"Karen"},{"orcid":"0000-0003-2279-1061","first_name":"Simon","id":"37B36620-F248-11E8-B48F-1D18A9856A87","last_name":"Hippenmeyer","full_name":"Hippenmeyer, Simon"},{"full_name":"Riezman, Howard","last_name":"Riezman","first_name":"Howard"},{"first_name":"Nikolaus","last_name":"Grigorieff","full_name":"Grigorieff, Nikolaus"},{"full_name":"Goode, Bruce","first_name":"Bruce","last_name":"Goode"}],"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."}],"language":[{"iso":"eng"}],"date_published":"2004-12-12T00:00:00Z","external_id":{"pmid":["15592479"]},"das_tickbox":"1","publication":"Nature Structural and Molecular Biology","publication_identifier":{"issn":["1545-9993"],"eissn":["1545-9985"]},"pmid":1,"status":"public","article_type":"original","title":"Conformational changes in the Arp2 3 complex leading to actin nucleation","intvolume":"        12","day":"12","user_id":"317138e5-6ab7-11ef-aa6d-ffef3953e345","date_updated":"2026-07-15T12:44:10Z","date_created":"2018-12-11T12:01:38Z","publist_id":"3554","fulldoi":"https://doi.org/10.1038/nsmb870","month":"12","publisher":"Nature Publishing Group","article_processing_charge":"No","_id":"3141"}