Evidence map›Paper›PMID 24573276›Full record

ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2014

Proteasome modulates positive and negative translational regulators in long-term synaptic plasticity.

Chenghai Dong, Svitlana V Bach, Kathryn A Haynes, Ashok N Hegde

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
5.4field-weighted citation impact, top 3% 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

38 citing papers in PubMed, 73 citations in OpenAlex.

  1. ACS chemical neuroscience · 2026
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  12. Synaptic control of DNA methylation involves activity-dependent degradation of DNMT3A1 in the nucleus.Neuropsychopharmacology : official publication of the American College of Neuropsychopharmacology · 2020
    Article
  13. Review
  14. Review
  15. Article
  16. Cell Clearing Systems Bridging Neuro-Immunity and Synaptic Plasticity.International journal of molecular sciences · 2019
    Review
  17. Article
  18. Article
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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

4 authors at 1 institution in 1 country.

Chenghai DongDepartment of Neurobiology and Anatomy, Wake Forest University Health Sciences, Medical Center Boulevard, Winston-Salem, North Carolina 27157.
Svitlana V Bach
Kathryn A Haynes
Ashok N Hegde
Wake Forest University · US

Funding

NINDS NIH HHS NS065583
6 · The paper itself

Abstract

Proteolysis by the ubiquitin-proteasome pathway appears to have a complex role in synaptic plasticity, but its various functions remain to be elucidated. Using late phase long-term potentiation (L-LTP) in the hippocampus of the mouse as a model for long-term synaptic plasticity, we previously showed that inhibition of the proteasome enhances induction but blocks maintenance of L-LTP. In this study, we investigated the possible mechanisms by which proteasome inhibition has opposite effects on L-LTP induction and maintenance. Our results show that inhibiting phosphatidyl inositol-3 kinase or blocking the interaction between eukaryotic initiation factors 4E (eIF4E) and 4G (eIF4G) reduces the enhancement of L-LTP induction brought about by proteasome inhibition suggesting interplay between proteolysis and the signaling pathway mediated by mammalian target of rapamycin (mTOR). Also, proteasome inhibition leads to accumulation of translational activators in the mTOR pathway such as eIF4E and eukaryotic elongation factor 1A (eEF1A) early during L-LTP causing increased induction. Furthermore, inhibition of the proteasome causes a buildup of translational repressors, such as polyadenylate-binding protein interacting protein 2 (Paip2) and eukaryotic initiation factor 4E-binding protein 2 (4E-BP2), during late stages of L-LTP contributing to the blockade of L-LTP maintenance. Thus, the proteasome plays a critical role in regulating protein synthesis during L-LTP by tightly controlling translation. Our results provide novel mechanistic insights into the interplay between protein degradation and protein synthesis in long-term synaptic plasticity.

Indexed as

AnimalsElectric StimulationEukaryotic Initiation Factor-4EEukaryotic Initiation Factor-4GHippocampusIn Vitro TechniquesLong-Term PotentiationMaleMiceMice, Inbred C57BLNeuronsPatch-Clamp TechniquesPhosphatidylinositol 3-KinasesProteasome Endopeptidase ComplexProteasome InhibitorsSignal TransductionEukaryotic Initiation Factor-4EEukaryotic Initiation Factor-4GmTOR protein, mousePhosphatidylinositol 3-KinasesProteasome Endopeptidase ComplexProteasome InhibitorsSirolimusTOR Serine-Threonine Kinasesactivatorlate-phase LTPprotein synthesisproteolysisrepressorubiquitin

Identifiers

PMID24573276
PMCPMC3935082
OpenAlexW1982210168

What OpenQuestion holds

Textmetadata
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.