Evidence map›Paper›PMID 31727973›Full record

ArticleScientific reports2019

Dendritic spine morphology and memory formation depend on postsynaptic Caskin proteins.

Norbert Bencsik, Szilvia Pusztai, Sándor Borbély, Anna Fekete, Metta Dülk, Viktor Kis, Szabolcs Pesti, Virág Vas, Attila Szűcs, László Buday and 1 more

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2019. 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
1.4field-weighted citation impact, top 21% 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, 30 citations in OpenAlex.

  1. CASKIN2 mediates PTPσ-orchestrated transsynaptic mechanisms at excitatory synapses.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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

11 authors at 4 institutions in 1 country.

Norbert BencsikDepartment of Physiology and Neurobiology, Eötvös Loránd University, Budapest, Hungary.
Szilvia PusztaiDepartment of Physiology and Neurobiology, Eötvös Loránd University, Budapest, Hungary.
Sándor BorbélyDepartment of Physiology and Neurobiology, Eötvös Loránd University, Budapest, Hungary.
Anna FeketeInstitute of Enzymology, Research Centre of Natural Sciences, Hungarian Academy of Sciences, Budapest, Hungary.
Metta DülkInstitute of Enzymology, Research Centre of Natural Sciences, Hungarian Academy of Sciences, Budapest, Hungary.
Viktor KisDepartment Anatomy, Cell and Developmental Biology, Eötvös Loránd University, Budapest, Hungary.
Szabolcs PestiDepartment Medical Chemistry, Semmelweis University, Budapest, Hungary.
Virág VasInstitute of Enzymology, Research Centre of Natural Sciences, Hungarian Academy of Sciences, Budapest, Hungary.
Attila SzűcsDepartment of Physiology and Neurobiology, Eötvös Loránd University, Budapest, Hungary.
László BudayInstitute of Enzymology, Research Centre of Natural Sciences, Hungarian Academy of Sciences, Budapest, Hungary.
Katalin SchlettDepartment of Physiology and Neurobiology, Eötvös Loránd University, Budapest, Hungary. schlett.katalin@ttk.elte.hu.
Eötvös Loránd University · HUHungarian Academy of Sciences · HUSemmelweis University · HUInstitute of Molecular Life Sciences · HU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

CASK-interactive proteins, Caskin1 and Caskin2, are multidomain neuronal scaffold proteins. Recent data from Caskin1 knockout animals indicated only a mild role of Caskin1 in anxiety and pain perception. In this work, we show that deletion of both Caskins leads to severe deficits in novelty recognition and spatial memory. Ultrastructural analyses revealed a reduction in synaptic profiles and dendritic spine areas of CA1 hippocampal pyramidal neurons of double knockout mice. Loss of Caskin proteins impaired LTP induction in hippocampal slices, while miniature EPSCs in dissociated hippocampal cultures appeared to be unaffected. In cultured Caskin knockout hippocampal neurons, overexpressed Caskin1 was enriched in dendritic spine heads and increased the amount of mushroom-shaped dendritic spines. Chemically induced LTP (cLTP) mediated enlargement of spine heads was augmented in the knockout mice and was not influenced by Caskin1. Immunocytochemistry and immunoprecipitation confirmed that Shank2, a master scaffold of the postsynaptic density, and Caskin1 co-localized within the same complex. Phosphorylation of AMPA receptors was specifically altered by Caskin deficiency and was not elevated by cLTP treatment further. Taken together, our results prove a previously unnoticed postsynaptic role of Caskin scaffold proteins and indicate that Caskins influence learning abilities via regulating spine morphology and AMPA receptor localisation.

Indexed as

Adaptor Proteins, Signal TransducingAnimalsCells, CulturedDendritic SpinesEmbryonic Stem CellsHippocampusMiceMice, KnockoutNerve Tissue ProteinsPrimary Cell CultureReceptors, AMPASpatial LearningSpatial MemoryAdaptor Proteins, Signal TransducingCaskin1 protein, mouseCaskin2 protein, mouseNerve Tissue ProteinsReceptors, AMPAShank2 protein, mouse

Identifiers

PMID31727973
PMCPMC6856520
OpenAlexW2982865882

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.