Evidence map›Paper›PMID 28670266›Full record

ArticleFrontiers in molecular neuroscience2017

GSK3α and GSK3β Phosphorylate Arc and Regulate its Degradation.

Agata Gozdz, Oleksii Nikolaienko, Malgorzata Urbanska, Iwona A Cymerman, Ewa Sitkiewicz, Magdalena Blazejczyk, Michal Dadlez, Clive R Bramham, Jacek Jaworski

Open access · goldAbstract read
In one paragraph

Article in Frontiers in molecular neuroscience, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
2.4field-weighted citation impact, top 12% 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

24 citing papers in PubMed, 37 citations in OpenAlex.

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  13. Effect of pharmacological manipulations on Arc function.Current research in pharmacology and drug discovery · 2021
    Review
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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

9 authors at 4 institutions in 2 countries.

Agata GozdzLaboratory of Molecular and Cellular Neurobiology, International Institute of Molecular and Cell BiologyWarsaw, Poland.
Oleksii NikolaienkoDepartment of Biomedicine and KG Jebsen Centre for Research on Neuropsychiatric Disorders, University of BergenBergen, Norway.
Malgorzata UrbanskaLaboratory of Molecular and Cellular Neurobiology, International Institute of Molecular and Cell BiologyWarsaw, Poland.
Iwona A CymermanLaboratory of Molecular and Cellular Neurobiology, International Institute of Molecular and Cell BiologyWarsaw, Poland.
Ewa SitkiewiczInstitute of Biochemistry and Biophysics, Polish Academy of ScienceWarsaw, Poland.
Magdalena BlazejczykLaboratory of Molecular and Cellular Neurobiology, International Institute of Molecular and Cell BiologyWarsaw, Poland.
Michal DadlezInstitute of Biochemistry and Biophysics, Polish Academy of ScienceWarsaw, Poland.
Clive R BramhamDepartment of Biomedicine and KG Jebsen Centre for Research on Neuropsychiatric Disorders, University of BergenBergen, Norway.
Jacek JaworskiLaboratory of Molecular and Cellular Neurobiology, International Institute of Molecular and Cell BiologyWarsaw, Poland.
International Institute of Molecular and Cell Biology · PLInstitute of Biochemistry and Biophysics, Polish Academy of Sciences · PLUniversity of Bergen · NOChildren's Memorial Health Institute · PL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The selective and neuronal activity-dependent degradation of synaptic proteins appears to be crucial for long-term synaptic plasticity. One such protein is activity-regulated cytoskeleton-associated protein (Arc), which regulates the synaptic content of α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptors (AMPAR), excitatory synapse strength and dendritic spine morphology. The levels of Arc protein are tightly regulated, and its removal occurs via proteasome-mediated degradation that requires prior ubiquitination. Glycogen synthase kinases α and β (GSK3α, GSKβ; collectively named GSK3α/β) are serine-threonine kinases with abundant expression in the central nervous system. Both GSK3 isozymes are tonically active under basal conditions, but their activity is regulated by intra- and extracellular factors, intimately involved in neuronal activity. Similar to Arc, GSK3α and GSK3β contribute to synaptic plasticity and the structural plasticity of dendritic spines. The present study identified Arc as a GSK3α/β substrate and showed that GSKβ promotes Arc degradation under conditions that induce

Indexed as

Arc/Arg3.1dendritic spinesGSK3neuronal activityNMDAphosphorylationproteasomal degradation

Identifiers

PMID28670266
PMCPMC5472658
OpenAlexW2621210398

What OpenQuestion holds

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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.