Evidence map›Paper›PMID 24465547›Full record

ArticlePloS one2014

Myosin II ATPase activity mediates the long-term potentiation-induced exodus of stable F-actin bound by drebrin A from dendritic spines.

Toshiyuki Mizui, Yuko Sekino, Hiroyuki Yamazaki, Yuta Ishizuka, Hideto Takahashi, Nobuhiko Kojima, Masami Kojima, Tomoaki Shirao

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
3.8field-weighted citation impact, top 7% 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

20 citing papers in PubMed, 48 citations in OpenAlex.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 2 institutions in 1 country.

Toshiyuki MizuiDepartment of Neurobiology and Behavior, Gunma University Graduate School of Medicine, Maebashi, Gunma, Japan ; Bio-interface Research Group, Health Research Institute, National Institute of Advanced Industrial Science and Technology (AIST), Ikeda, Osaka, Japan.
Yuko SekinoDepartment of Neurobiology and Behavior, Gunma University Graduate School of Medicine, Maebashi, Gunma, Japan ; Core Research for Evolution Science and Technology, Japan Science and Technology Corporation, Kawaguchi, Saitama, Japan.
Hiroyuki YamazakiDepartment of Neurobiology and Behavior, Gunma University Graduate School of Medicine, Maebashi, Gunma, Japan.
Yuta IshizukaDepartment of Neurobiology and Behavior, Gunma University Graduate School of Medicine, Maebashi, Gunma, Japan.
Hideto TakahashiDepartment of Neurobiology and Behavior, Gunma University Graduate School of Medicine, Maebashi, Gunma, Japan.
Nobuhiko KojimaDepartment of Neurobiology and Behavior, Gunma University Graduate School of Medicine, Maebashi, Gunma, Japan.
Masami KojimaCore Research for Evolution Science and Technology, Japan Science and Technology Corporation, Kawaguchi, Saitama, Japan ; Bio-interface Research Group, Health Research Institute, National Institute of Advanced Industrial Science and Technology (AIST), Ikeda, Osaka, Japan.
Tomoaki ShiraoDepartment of Neurobiology and Behavior, Gunma University Graduate School of Medicine, Maebashi, Gunma, Japan.
Gunma University · JPNational Institute of Advanced Industrial Science and Technology · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The neuronal actin-binding protein drebrin A forms a stable structure with F-actin in dendritic spines. NMDA receptor activation causes an exodus of F-actin bound by drebrin A (DA-actin) from dendritic spines, suggesting a pivotal role for DA-actin exodus in synaptic plasticity. We quantitatively assessed the extent of DA-actin localization to spines using the spine-dendrite ratio of drebrin A in cultured hippocampal neurons, and found that (1) chemical long-term potentiation (LTP) stimulation induces rapid DA-actin exodus and subsequent DA-actin re-entry in dendritic spines, (2) Ca(2+) influx through NMDA receptors regulates the exodus and the basal accumulation of DA-actin, and (3) the DA-actin exodus is blocked by myosin II ATPase inhibitor, but is not blocked by myosin light chain kinase (MLCK) or Rho-associated kinase (ROCK) inhibitors. These results indicate that myosin II mediates the interaction between NMDA receptor activation and DA-actin exodus in LTP induction. Furthermore, myosin II seems to be activated by a rapid actin-linked mechanism rather than slow MLC phosphorylation. Thus the myosin-II mediated DA-actin exodus might be an initial event in LTP induction, triggering actin polymerization and spine enlargement.

Indexed as

ActinsAdenosine TriphosphatasesAnimalsBicucullineCalciumCells, CulturedDendritic SpinesFemaleGABA-A Receptor AntagonistsGlutamic AcidGlycineHippocampusLong-Term PotentiationMicroscopy, FluorescenceMyosin Type IINeuronsActinsAdenosine TriphosphatasesBicucullineCalciumdrebrinsGABA-A Receptor AntagonistsGlutamic AcidGlycineMyosin Type IINeuropeptidesReceptors, N-Methyl-D-AspartateTetrodotoxin

Identifiers

PMID24465547
PMCPMC3899004
OpenAlexW2023702220

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

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.