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We show that Spire\u2013actin complexes in solution assume a unique, longitudinal-like shape, in which Wiskott\u2013Aldrich syndrome protein homology 2 domains (WH2), in an extended configuration, line up actins along the long axis of the core of the Spire\u2013actin particle. In the complex, the kinase noncatalytic C-lobe domain is positioned at the side of the first N-terminal Spire\u2013actin module. In addition, we find that preformed, isolated Spire\u2013actin complexes are very efficient nucleators of polymerization and afterward dissociate from the growing filament. However, under certain conditions, all Spire constructs\u2014even a single WH2 repeat\u2014sequester actin and disrupt existing filaments. This molecular and structural mechanism of actin polymerization by Spire should apply to other actin-binding proteins that contain WH2 domains in tandem.<\/jats:p>","DOI":"10.1073\/pnas.1115465108","type":"journal-article","created":{"date-parts":[[2011,11,22]],"date-time":"2011-11-22T02:22:31Z","timestamp":1321928551000},"page":"19575-19580","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":28,"title":["Molecular architecture of the Spire\u2013actin nucleus and its implication for actin filament assembly"],"prefix":"10.1073","volume":"108","author":[{"given":"Tomasz","family":"Sitar","sequence":"first","affiliation":[{"name":"Max Planck Institute of Biochemistry, 82152 Martinsried, Germany;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Julia","family":"Gallinger","sequence":"additional","affiliation":[{"name":"Institute for Anatomy and Cell Biology, Ludwig-Maximilians University, Schillerstrasse 42, 80336 Munich, 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