ArticleProceedings of the National Academy of Sciences of the United States of America2008
X-ray scattering study of actin polymerization nuclei assembled by tandem W domains.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
What it found
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Who cites it
18 citing papers in PubMed.
- Functional Mimicry of Eukaryotic Actin Assembly by Pathogen Effector Proteins.International journal of molecular sciences · 2022Review
- The WH2 Domain and Actin Nucleation: Necessary but Insufficient.Trends in biochemical sciences · 2016Review
- Biochemical Activities of the Wiskott-Aldrich Syndrome Homology Region 2 Domains of Sarcomere Length Short (SALS) Protein.The Journal of biological chemistry · 2016Article
- Specification of Architecture and Function of Actin Structures by Actin Nucleation Factors.Annual review of biophysics · 2015Review
- Processive acceleration of actin barbed-end assembly by N-WASP.Molecular biology of the cell · 2014Article
- Structural basis of actin filament nucleation by tandem W domains.Cell reports · 2013Article
- Interactions of isolated C-terminal fragments of neural Wiskott-Aldrich syndrome protein (N-WASP) with actin and Arp2/3 complex.The Journal of biological chemistry · 2012Article
- Molecular architecture of the Spire-actin nucleus and its implication for actin filament assembly.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Spire-type actin nucleators cooperate with Formin-2 to drive asymmetric oocyte division.Current biology : CB · 2011Article
- New mechanisms and functions of actin nucleation.Current opinion in cell biology · 2011Review
- Structure of a longitudinal actin dimer assembled by tandem w domains: implications for actin filament nucleation.Journal of molecular biology · 2010Article
- Structures of actin-bound Wiskott-Aldrich syndrome protein homology 2 (WH2) domains of Spire and the implication for filament nucleation.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Actin complexes in the cell nucleus: new stones in an old field.Histochemistry and cell biology · 2010Review
- A nucleator arms race: cellular control of actin assembly.Nature reviews. Molecular cell biology · 2010Review
- Structural insights into de novo actin polymerization.Current opinion in structural biology · 2010Review
- Actin oligomers at the initial stage of polymerization induced by increasing temperature at low ionic strength: Study with small-angle X-ray scattering.Biophysics (Nagoya-shi, Japan) · 2010Article
- Inside view of cell locomotion through single-molecule: fast F-/G-actin cycle and G-actin regulation of polymer restoration.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2010Review
- Actin filament nucleation and elongation factors--structure-function relationships.Critical reviews in biochemistry and molecular biologyReview
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
The initiation of actin polymerization in cells requires actin filament nucleators. With the exception of formins, known filament nucleators use the Wiskott-Aldrich syndrome protein (WASP) homology 2 (WH2 or W) domain for interaction with actin. A common architecture, found in Spire, Cobl, VopL, and VopF, consists of tandem W domains that tie together three to four actin monomers to form a polymerization nucleus. Uncontrollable polymerization has prevented the structural investigation of such nuclei. We have engineered stable nuclei consisting of an actin dimer and a trimer stabilized by tandem W domain hybrid constructs and studied their structures in solution by x-ray scattering. We show that Spire-like tandem W domains stabilize a polymerization nucleus by lining up actin subunits along the long-pitch helix of the actin filament. Intersubunit contacts in the polymerization nucleus, thought to involve the DNase I-binding loop of actin, coexist with the binding of the W domain in the cleft between actin subdomains 1 and 3. The successful stabilization of filament-like multiactin assemblies opens the way to the crystallographic investigation of intersubunit contacts in the actin filament.
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