Evidence map›Paper›PMID 25293574›Full record

ArticleThe EMBO journal2014

Nanoscale segregation of actin nucleation and elongation factors determines dendritic spine protrusion.

Anaël Chazeau, Amine Mehidi, Deepak Nair, Jérémie J Gautier, Cécile Leduc, Ingrid Chamma, Frieda Kage, Adel Kechkar, Olivier Thoumine, Klemens Rottner and 4 more

Open access · greenAbstract read
In one paragraph

Article in The EMBO journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 75 papers.

0numbers the graph read from it
0cells of the map it votes in
75citing papers in PubMed
6.8field-weighted citation impact, top 2% 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

75 citing papers in PubMed, 141 citations in OpenAlex.

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  16. Unraveling the mysteries of dendritic spine dynamics: Five key principles shaping memory and cognition.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2023
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15 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

14 authors at 3 institutions in 2 countries.

Anaël ChazeauInterdisciplinary Institute for Neuroscience, University Bordeaux UMR 5297, Bordeaux, France CNRS, Interdisciplinary Institute for Neuroscience UMR 5297, Bordeaux, France.
Amine MehidiInterdisciplinary Institute for Neuroscience, University Bordeaux UMR 5297, Bordeaux, France CNRS, Interdisciplinary Institute for Neuroscience UMR 5297, Bordeaux, France.
Deepak NairInterdisciplinary Institute for Neuroscience, University Bordeaux UMR 5297, Bordeaux, France CNRS, Interdisciplinary Institute for Neuroscience UMR 5297, Bordeaux, France.
Jérémie J GautierCNRS UPR3082, Laboratoire d'Enzymologie et Biochimie Structurales, Gif-sur-Yvette Cedex, France.
Cécile LeducUniversity Bordeaux, LP2N, Talence, France CNRS & Institut d'Optique, LP2N, Talence, France.
Ingrid ChammaInterdisciplinary Institute for Neuroscience, University Bordeaux UMR 5297, Bordeaux, France CNRS, Interdisciplinary Institute for Neuroscience UMR 5297, Bordeaux, France.
Frieda KageDivision of Molecular Cell Biology, Zoological Institute, Technical University Braunschweig, Braunschweig, Germany.
Adel KechkarInterdisciplinary Institute for Neuroscience, University Bordeaux UMR 5297, Bordeaux, France CNRS, Interdisciplinary Institute for Neuroscience UMR 5297, Bordeaux, France.
Olivier ThoumineInterdisciplinary Institute for Neuroscience, University Bordeaux UMR 5297, Bordeaux, France CNRS, Interdisciplinary Institute for Neuroscience UMR 5297, Bordeaux, France.
Klemens RottnerDivision of Molecular Cell Biology, Zoological Institute, Technical University Braunschweig, Braunschweig, Germany Helmholtz Centre for Infection Research, Braunschweig, Germany.
Daniel ChoquetInterdisciplinary Institute for Neuroscience, University Bordeaux UMR 5297, Bordeaux, France CNRS, Interdisciplinary Institute for Neuroscience UMR 5297, Bordeaux, France.
Alexis GautreauCNRS UPR3082, Laboratoire d'Enzymologie et Biochimie Structurales, Gif-sur-Yvette Cedex, France.
Jean-Baptiste SibaritaInterdisciplinary Institute for Neuroscience, University Bordeaux UMR 5297, Bordeaux, France CNRS, Interdisciplinary Institute for Neuroscience UMR 5297, Bordeaux, France.
Grégory GiannoneInterdisciplinary Institute for Neuroscience, University Bordeaux UMR 5297, Bordeaux, France CNRS, Interdisciplinary Institute for Neuroscience UMR 5297, Bordeaux, France gregory.giannone@u-bordeaux2.fr.
Centre National de la Recherche Scientifique · FRHelmholtz Centre for Infection Research · DETechnische Universität Braunschweig · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Actin dynamics drive morphological remodeling of neuronal dendritic spines and changes in synaptic transmission. Yet, the spatiotemporal coordination of actin regulators in spines is unknown. Using single protein tracking and super-resolution imaging, we revealed the nanoscale organization and dynamics of branched F-actin regulators in spines. Branched F-actin nucleation occurs at the PSD vicinity, while elongation occurs at the tip of finger-like protrusions. This spatial segregation differs from lamellipodia where both branched F-actin nucleation and elongation occur at protrusion tips. The PSD is a persistent confinement zone for IRSp53 and the WAVE complex, an activator of the Arp2/3 complex. In contrast, filament elongators like VASP and formin-like protein-2 move outwards from the PSD with protrusion tips. Accordingly, Arp2/3 complexes associated with F-actin are immobile and surround the PSD. Arp2/3 and Rac1 GTPase converge to the PSD, respectively, by cytosolic and free-diffusion on the membrane. Enhanced Rac1 activation and Shank3 over-expression, both associated with spine enlargement, induce delocalization of the WAVE complex from the PSD. Thus, the specific localization of branched F-actin regulators in spines might be reorganized during spine morphological remodeling often associated with synaptic plasticity.

Indexed as

Models, BiologicalActin-Related Protein 2-3 ComplexActinsAdaptor Proteins, Signal TransducingAnimalsCells, CulturedDendritic SpinesForminsNerve Tissue ProteinsPolymerase Chain ReactionPost-Synaptic DensityProteinsRatsRats, Sprague-DawleyStatistics, NonparametricSynaptic TransmissionActin-Related Protein 2-3 ComplexActinsAdaptor Proteins, Signal TransducingBaiap2 protein, ratFMNL2 protein, humanForminsNerve Tissue ProteinsProteinsbranched F‐actin regulatorsdendritic spinepostsynaptic densitysingle protein trackingsuper‐resolution microscopy

Identifiers

PMID25293574
PMCPMC4282554
OpenAlexW1986448286

What OpenQuestion holds

Textmetadata
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Registered trials

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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.