Evidence map›Paper›PMID 22106272›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2011

Molecular architecture of the Spire-actin nucleus and its implication for actin filament assembly.

Tomasz Sitar, Julia Gallinger, Anna M Ducka, Teemu P Ikonen, Michael Wohlhoefler, Kurt M Schmoller, Andreas R Bausch, Peteranne Joel, Kathleen M Trybus, Angelika A Noegel and 3 more

Erratum issuedOpen access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.8field-weighted citation impact, top 17% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

16 citing papers in PubMed, 30 citations in OpenAlex.

  1. Life science alliance · 2026
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  7. Spire1 and Myosin Vc promote CaCellular and molecular life sciences : CMLS · 2022
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  9. Review
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  15. Ablation of cyclase-associated protein 2 (CAP2) leads to cardiomyopathy.Cellular and molecular life sciences : CMLS · 2013
    Article
  16. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

13 authors at 7 institutions in 4 countries.

Tomasz SitarMax Planck Institute of Biochemistry, 82152 Martinsried, Germany. sitar@biochem.mpg.de
Julia Gallinger
Anna M Ducka
Teemu P Ikonen
Michael Wohlhoefler
Kurt M Schmoller
Andreas R Bausch
Peteranne Joel
Kathleen M Trybus
Angelika A Noegel
Michael Schleicher
Robert Huber
Tad A Holak
Max Planck Society · DETechnical University of Munich · DELudwig-Maximilians-Universität München · DEUniversity of Vermont · USMax Planck Institute of Biochemistry · DEPaul Scherrer Institute · CHUniversity of Cologne · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

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.

Indexed as

Actin CytoskeletonActinsAnimalsBinding SitesCrystallography, X-RayDrosophila melanogasterDrosophila ProteinsElectrophoresis, Polyacrylamide GelMicrofilament ProteinsMicroscopy, FluorescenceModels, MolecularMultiprotein ComplexesProtein BindingProtein Structure, TertiaryScattering, Small AngleTandem Repeat SequencesActinsDrosophila ProteinsMicrofilament ProteinsMultiprotein Complexesspir protein, DrosophilaWiskott-Aldrich Syndrome Protein Family

Identifiers

PMID22106272
PMCPMC3241762
OpenAlexW2037565201

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.