Evidence map›Paper›PMID 25018696›Full record

ReviewFrontiers in molecular neuroscience2014

Protein degradation and protein synthesis in long-term memory formation.

Timothy J Jarome, Fred J Helmstetter

Open access · goldAbstract readReview
In one paragraph

Review in Frontiers in molecular neuroscience, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers.

0numbers the graph read from it
0cells of the map it votes in
70citing papers in PubMed
4.0field-weighted citation impact, top 5% 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

70 citing papers in PubMed, 121 citations in OpenAlex.

  1. Article
  2. Review
  3. HomozygousThe Yale journal of biology and medicine · 2026
    Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. DNA Methylation in Long-Term Memory.Physiology (Bethesda, Md.) · 2025
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Muscarinic receptor activation overrides boundary conditions on memory updating in a calcium/calmodulin-dependent manner.Neuropsychopharmacology : official publication of the American College of Neuropsychopharmacology · 2023
    Article
  16. Article
  17. Article
  18. The immune system as a system of relations.Frontiers in immunology · 2022
    Review
  19. Article
  20. Review

10 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

2 authors at 1 institution in 1 country.

Timothy J JaromeDepartment of Neurobiology, University of Alabama at Birmingham Birmingham, AL, USA ; Department of Psychology, University of Wisconsin-Milwaukee Milwaukee, WI, USA.
Fred J HelmstetterDepartment of Psychology, University of Wisconsin-Milwaukee Milwaukee, WI, USA.
University of Wisconsin–Milwaukee · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Long-term memory (LTM) formation requires transient changes in the activity of intracellular signaling cascades that are thought to regulate new gene transcription and de novo protein synthesis in the brain. Consistent with this, protein synthesis inhibitors impair LTM for a variety of behavioral tasks when infused into the brain around the time of training or following memory retrieval, suggesting that protein synthesis is a critical step in LTM storage in the brain. However, evidence suggests that protein degradation mediated by the ubiquitin-proteasome system (UPS) may also be a critical regulator of LTM formation and stability following retrieval. This requirement for increased protein degradation has been shown in the same brain regions in which protein synthesis is required for LTM storage. Additionally, increases in the phosphorylation of proteins involved in translational control parallel increases in protein polyubiquitination and the increased demand for protein degradation is regulated by intracellular signaling molecules thought to regulate protein synthesis during LTM formation. In some cases inhibiting proteasome activity can rescue memory impairments that result from pharmacological blockade of protein synthesis, suggesting that protein degradation may control the requirement for protein synthesis during the memory storage process. Results such as these suggest that protein degradation and synthesis are both critical for LTM formation and may interact to properly "consolidate" and store memories in the brain. Here, we review the evidence implicating protein synthesis and degradation in LTM storage and highlight the areas of overlap between these two opposing processes. We also discuss evidence suggesting these two processes may interact to properly form and store memories. LTM storage likely requires a coordinated regulation between protein degradation and synthesis at multiple sites in the mammalian brain.

Indexed as

amygdalafear conditioninghippocampusproteasomeprotein degradationprotein synthesisubiquitin

Identifiers

PMID25018696
PMCPMC4072070
OpenAlexW2015109916

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.