Evidence map›Paper›PMID 23342115›Full record

ArticlePloS one2013

SPIN90 phosphorylation modulates spine structure and synaptic function.

In Ha Cho, Dae Hwan Kim, Min-Jung Lee, Jeomil Bae, Kun Ho Lee, Woo Keun Song

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed, 1 pooled it
0.6field-weighted citation impact, top 39% 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

13 citing papers in PubMed, 1 synthesis or guideline pooled it, 21 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Arp2/3-mediated bidirectional actin assembly by SPIN90 dimers.Nature structural & molecular biology · 2025
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Local substrates of non-receptor tyrosine kinases at synaptic sites in neurons.Sheng li xue bao : [Acta physiologica Sinica] · 2017
    Review
  11. Article
  12. Review
  13. Article
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

6 authors at 2 institutions in 1 country.

In Ha ChoBio Imaging and Cell Dynamics Center, School of Life Sciences, Gwangju Institute of Science and Technology, Gwangju, Korea.
Dae Hwan Kim
Min-Jung Lee
Jeomil Bae
Kun Ho Lee
Woo Keun Song
Gwangju Institute of Science and Technology · KRChosun University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The correct rearrangement of postsynaptic components in dendritic spines is important for driving changes of spine structure and synaptic function. SPIN90 plays an essential role in many cellular processes including actin polymerization, endocytosis, growth cone formation and dendritic spine morphogenesis. Here, we demonstrate that SPIN90, which is a binding partner of PSD95 and Shank in spines, is targeted to synapses and leads to enhanced synaptic activity in neurons. We show, using in vitro and in vivo kinase assays, that SPIN90 is tyrosine phosphorylated by Src kinase. SPIN90 that was tyrosine-phosphorylated by Src was targeted to dendritic spines in cultured hippocampal neurons. Moreover, a SPIN90 phospho-deficient mutant was unable to accumulate at dendritic spines whereas SPIN90 WT and a phospho-mimicking mutant were localized at spines and bound PSD95 and Shank with increased efficiency. Consistent with these findings, hippocampal neurons that overexpressed SPIN90 WT or a phospho-mimicking mutant had enlarged spine heads, leading to enhanced postsynaptic function in terms of both amplitude and frequency. Together, our findings show that SPIN90 modulates synaptic activity in neurons as a result of its phosphorylation.

Indexed as

Adaptor Proteins, Signal TransducingAnimalsBlotting, WesternCell LineCells, CulturedChlorocebus aethiopsCOS CellsElectrophysiologyHippocampusHumansImmunoprecipitationMuscle ProteinsNerve Tissue ProteinsNeuronsPhosphorylationSpineAdaptor Proteins, Signal TransducingMuscle ProteinsNCKIPSD protein, humanNerve Tissue ProteinsSPIN90 protein, mouse

Identifiers

PMID23342115
PMCPMC3544810
OpenAlexW1994857914

What OpenQuestion holds

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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.