{"status":"public","title":"Conformational changes in the Arp2 3 complex leading to actin nucleation","quality_controlled":0,"year":"2005","publisher":"Nature Publishing Group","publist_id":"3554","date_created":"2018-12-11T12:01:38Z","volume":12,"intvolume":"        12","abstract":[{"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.","lang":"eng"}],"_id":"3141","issue":"1","extern":1,"date_published":"2005-01-01T00:00:00Z","publication_status":"published","citation":{"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>. 2005;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. 2005. Conformational changes in the Arp2 3 complex leading to actin nucleation. Nature Structural and Molecular Biology. 12(1), 26–31.","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, 2005. <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. (2005). 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>","short":"A. Rodal, O. Sokolova, D. Robins, K. Daugherty, S. Hippenmeyer, H. Riezman, N. Grigorieff, B. Goode, Nature Structural and Molecular Biology 12 (2005) 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, 2005, pp. 26–31, doi:<a href=\"https://doi.org/10.1038/nsmb870\">10.1038/nsmb870</a>.","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, 2005."},"date_updated":"2021-01-12T07:41:21Z","month":"01","author":[{"full_name":"Rodal, Avital A","first_name":"Avital","last_name":"Rodal"},{"last_name":"Sokolova","first_name":"Olga","full_name":"Sokolova, Olga"},{"last_name":"Robins","first_name":"Deborah","full_name":"Robins, Deborah B"},{"last_name":"Daugherty","first_name":"Karen","full_name":"Daugherty, Karen M"},{"full_name":"Simon Hippenmeyer","id":"37B36620-F248-11E8-B48F-1D18A9856A87","last_name":"Hippenmeyer","first_name":"Simon","orcid":"0000-0003-2279-1061"},{"first_name":"Howard","last_name":"Riezman","full_name":"Riezman, Howard"},{"last_name":"Grigorieff","first_name":"Nikolaus","full_name":"Grigorieff, Nikolaus"},{"full_name":"Goode, Bruce L","last_name":"Goode","first_name":"Bruce"}],"day":"01","publication":"Nature Structural and Molecular Biology","doi":"10.1038/nsmb870","page":"26 - 31","type":"journal_article"}