NDLI: Molecular architecture of the Spire–actin nucleus and its implication for actin filament assembly

Content Provider	PubMed Central
Author	Sitar, Tomasz Gallinger, Julia Ducka, Anna M. Ikonen, Teemu P. Michael, Wohlhoefler Schmoller, Kurt M. Bausch, Andreas R. Joel, Peteranne Trybus, Kathleen M. Noegel, Angelika A. Schleicher, Michael Huber, Robert Holak, Tad A.
Abstract	The Spire protein is a multifunctional regulator of actin assembly. We studied the structures and properties of Spire–actin complexes by X-ray scattering, X-ray crystallography, total internal reflection fluorescence microscopy, and actin polymerization assays. We show that Spire–actin complexes in solution assume a unique, longitudinal-like shape, in which Wiskott–Aldrich syndrome protein homology 2 domains (WH2), in an extended configuration, line up actins along the long axis of the core of the Spire–actin particle. In the complex, the kinase noncatalytic C-lobe domain is positioned at the side of the first N-terminal Spire–actin module. In addition, we find that preformed, isolated Spire–actin complexes are very efficient nucleators of polymerization and afterward dissociate from the growing filament. However, under certain conditions, all Spire constructs—even a single WH2 repeat—sequester 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.
Related Links	http://dx.doi.org/10.1073/pnas.1115465108
Ending Page	19580
Page Count	6
Starting Page	19575
File Format	PDF
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	49
Volume Number	108
Language	English
Publisher	National Academy of Sciences
Publisher Date	2011-12-06
Access Restriction	Open
Rights Holder	National Academy of Sciences
Subject Keyword	General Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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