Evidence map›Paper›PMID 18441292›Full record

ArticleLearning & memory (Cold Spring Harbor, N.Y.)2008

Proteasome inhibition enhances the induction and impairs the maintenance of late-phase long-term potentiation.

Chenghai Dong, Sudarshan C Upadhya, Lan Ding, Thuy K Smith, Ashok N Hegde

Open access · diamondAbstract read
In one paragraph

Article in Learning & memory (Cold Spring Harbor, N.Y.), 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 89 papers.

0numbers the graph read from it
0cells of the map it votes in
89citing papers in PubMed
–field-weighted citation impact
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

89 citing papers in PubMed, 157 citations in OpenAlex.

  1. ACS chemical neuroscience · 2026
    Article
  2. Article
  3. Review
  4. The Ubiquitin-Proteasome System in Brain Disorders: Pathogenic Pathways, Post-Translational Tweaks, and Therapeutic Frontiers.Journal of neuroimmune pharmacology : the official journal of the Society on NeuroImmune Pharmacology · 2025
    Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Review
  12. Proteasome localization and activity in pig brain andFrontiers in cellular neuroscience · 2024
    Article
  13. Article
  14. Review
  15. Review
  16. Article
  17. Review
  18. Article
  19. Article
  20. Article

29 more citing papers are in PubMed but not listed here.

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

5 authors at 1 institution in 1 country.

Chenghai DongDepartment of Neurobiology and Anatomy, Wake Forest University Health Sciences, Winston-Salem, North Carolina 27157, USA.
Sudarshan C Upadhya
Lan Ding
Thuy K Smith
Ashok N Hegde
Wake Forest University · US

Funding

REGULATED PROTEOLYSIS AND LONG-TERM MEMORYR01MH060225 · NIMH · WAKE FOREST UNIVERSITY HEALTH SCIENCES · PI HEGDE, ASHOK N · 2000 to 2010
$2.4M
NIMH NIH HHS MH060225NIMH NIH HHS R01 MH060225
6 · The paper itself

Abstract

Protein degradation by the ubiquitin-proteasome pathway plays important roles in synaptic plasticity, but the molecular mechanisms by which proteolysis regulates synaptic strength are not well understood. We investigated the role of the proteasome in hippocampal late-phase long-term potentiation (L-LTP), a model for enduring synaptic plasticity. We show here that inhibition of the proteasome enhances the induction of L-LTP, but inhibits its maintenance. Proteasome inhibitor-mediated enhancement of the early part of L-LTP requires activation of NMDA receptors and the cAMP-dependent protein kinase. Augmentation of L-LTP induction by proteasome inhibition is blocked by a protein synthesis inhibitor anisomycin and is sensitive to the drug rapamycin. Our findings indicate that proteasome inhibition increases the induction of L-LTP by stabilizing locally translated proteins in dendrites. In addition, our data show that inhibition of the proteasome blocks transcription of brain-derived neurotrophic factor (BDNF), which is a cAMP-responsive element-binding protein (CREB)-inducible gene. Furthermore, our results demonstrate that the proteasome inhibitors block degradation of ATF4, a CREB repressor. Thus, proteasome inhibition appears to hinder CREB-mediated transcription. Our results indicate that blockade of proteasome activity obstructs the maintenance of L-LTP by interfering with transcription as well as translation required to sustain L-LTP. Thus, proteasome-mediated proteolysis has different roles during the induction and the maintenance of L-LTP.

Indexed as

Proteasome InhibitorsAnimalsAnisomycinBrain-Derived Neurotrophic FactorCyclic AMP-Dependent Protein KinasesCyclic AMP Response Element-Binding ProteinDendritesHippocampusLong-Term PotentiationMiceNeuronal PlasticityPeptide HydrolasesProtein BiosynthesisProtein Synthesis InhibitorsReceptors, N-Methyl-D-AspartateRNA, MessengerAnisomycinBrain-Derived Neurotrophic FactorCyclic AMP-Dependent Protein KinasesCyclic AMP Response Element-Binding ProteinPeptide HydrolasesProteasome InhibitorsProtein Synthesis InhibitorsReceptors, N-Methyl-D-AspartateRNA, MessengerUbiquitin

Identifiers

PMID18441292
PMCPMC2364605
OpenAlexW2050711545

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.