Evidence map›Paper›PMID 24586110›Full record

ArticlePLoS biology2014

Spire and Formin 2 synergize and antagonize in regulating actin assembly in meiosis by a ping-pong mechanism.

Pierre Montaville, Antoine Jégou, Julien Pernier, Christel Compper, Bérengère Guichard, Binyam Mogessie, Melina Schuh, Guillaume Romet-Lemonne, Marie-France Carlier

Open access · goldAbstract read
In one paragraph

Article in PLoS biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
5.5field-weighted citation impact, top 4% 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

48 citing papers in PubMed, 92 citations in OpenAlex.

  1. From Cytoskeletal Remodeling to Oocyte Quality: The Emerging Role of Mechanics.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Review
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  10. Antagonistic Activities of Fmn2 and ADF Regulate Axonal F-Actin Patch Dynamics and the Initiation of Collateral Branching.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2022
    Article
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  12. Article
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  18. The advantages of microfluidics to study actin biochemistry and biomechanics.Journal of muscle research and cell motility · 2020
    Review
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors at 3 institutions in 2 countries.

Pierre MontavilleLaboratoire d'Enzymologie et Biochimie Structurale, CNRS, Gif-sur-Yvette, France.
Antoine JégouLaboratoire d'Enzymologie et Biochimie Structurale, CNRS, Gif-sur-Yvette, France.
Julien PernierLaboratoire d'Enzymologie et Biochimie Structurale, CNRS, Gif-sur-Yvette, France.
Christel CompperLaboratoire d'Enzymologie et Biochimie Structurale, CNRS, Gif-sur-Yvette, France.
Bérengère GuichardLaboratoire d'Enzymologie et Biochimie Structurale, CNRS, Gif-sur-Yvette, France.
Binyam MogessieMRC Laboratory of Molecular Biology, Cambridge, United Kingdom.
Melina SchuhMRC Laboratory of Molecular Biology, Cambridge, United Kingdom.
Guillaume Romet-LemonneLaboratoire d'Enzymologie et Biochimie Structurale, CNRS, Gif-sur-Yvette, France.
Marie-France CarlierLaboratoire d'Enzymologie et Biochimie Structurale, CNRS, Gif-sur-Yvette, France.
Laboratoire d'Enzymologie et Biochimie Structurales · FRCentre National de la Recherche Scientifique · FRMRC Laboratory of Molecular Biology · GB

Funding

Medical Research Council MC_U105192711
6 · The paper itself

Abstract

In mammalian oocytes, three actin binding proteins, Formin 2 (Fmn2), Spire, and profilin, synergistically organize a dynamic cytoplasmic actin meshwork that mediates translocation of the spindle toward the cortex and is required for successful fertilization. Here we characterize Fmn2 and elucidate the molecular mechanism for this synergy, using bulk solution and individual filament kinetic measurements of actin assembly dynamics. We show that by capping filament barbed ends, Spire recruits Fmn2 and facilitates its association with barbed ends, followed by rapid processive assembly and release of Spire. In the presence of actin, profilin, Spire, and Fmn2, filaments display alternating phases of rapid processive assembly and arrested growth, driven by a "ping-pong" mechanism, in which Spire and Fmn2 alternately kick off each other from the barbed ends. The results are validated by the effects of injection of Spire, Fmn2, and their interacting moieties in mouse oocytes. This original mechanism of regulation of a Rho-GTPase-independent formin, recruited by Spire at Rab11a-positive vesicles, supports a model for modulation of a dynamic actin-vesicle meshwork in the oocyte at the origin of asymmetric positioning of the meiotic spindle.

Indexed as

MeiosisActinsAnimalsCells, CulturedFeedback, PhysiologicalForminsHumansKineticsMiceMicrofilament ProteinsNerve Tissue ProteinsNuclear ProteinsOocytesProfilinsProtein BindingProtein MultimerizationActinsformin 2 protein, mouseForminsMicrofilament ProteinsNerve Tissue ProteinsNuclear ProteinsProfilinsSPIRE1 protein, human

Identifiers

PMID24586110
PMCPMC3934834
OpenAlexW2065359530

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.