Evidence map›Paper›PMID 32745599›Full record

ReviewNeurobiology of learning and memory2020

The diversity of linkage-specific polyubiquitin chains and their role in synaptic plasticity and memory formation.

Madeline Musaus, Shaghayegh Navabpour, Timothy J Jarome

Abstract readReview
In one paragraph

Review in Neurobiology of learning and memory, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing 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

21 citing papers in PubMed.

  1. Article
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  3. Article
  4. Review
  5. Article
  6. Review
  7. Article
  8. Emerging roles for E3 ubiquitin ligases in neural development and disease.Frontiers in cell and developmental biology · 2025
    Review
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. Review
  16. 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

3 authors.

Madeline MusausSchool of Neuroscience, Virginia Polytechnic Institute and State University, Blacksburg, VA, USA.
Shaghayegh NavabpourFralin Biomedical Research Institute, Translational Biology, Medicine and Health, Virginia Polytechnic Institute and State University, Roanoke, VA, USA.
Timothy J JaromeSchool of Neuroscience, Virginia Polytechnic Institute and State University, Blacksburg, VA, USA; Fralin Biomedical Research Institute, Translational Biology, Medicine and Health, Virginia Polytechnic Institute and State University, Roanoke, VA, USA; Department of Animal and Poultry Sciences, Virginia Polytechnic Institute and State University, Blacksburg, VA, USA. Electronic address: tjjarome@vt.edu.

Funding

The role of linear ubiquitination in memory formationR21MH120569 · NIMH · VIRGINIA POLYTECHNIC INST AND ST UNIV · PI JAROME, TIMOTHY JOSEPH · 2020 to 2021
$422k
Exploring epigenetic regulation of memory extinctionR21MH120498 · NIMH · VIRGINIA POLYTECHNIC INST AND ST UNIV · PI JAROME, TIMOTHY JOSEPH, XIE, HEHUANG · 2020 to 2020
$419k
NIMH NIH HHS R21 MH120498NIMH NIH HHS R21 MH120569
6 · The paper itself

Abstract

Over the last 20 years, a number of studies have provided strong support for protein degradation mediated by the ubiquitin-proteasome system in synaptic plasticity and memory formation. In this system, target substrates become covalently modified by the small protein ubiquitin through a series of enzymatic reactions involving hundreds of different ligases. While some substrates will acquire only a single ubiquitin, most will be marked by multiple ubiquitin modifications, which link together at specific lysine sites or the N-terminal methionine on the previous ubiquitin to form a polyubiquitin chain. There are at least eight known linkage-specific polyubiquitin chains a target protein can acquire, many of which are independent of the proteasome, and these chains can be homogenous, mixed, or branched in nature, all of which result in different functional outcomes and fates for the target substrate. However, as the focus has remained on protein degradation, much remains unknown about the role of these diverse ubiquitin chains in the brain, particularly during activity- and learning-dependent synaptic plasticity. Here, we review the different types and functions of ubiquitin chains and summarize evidence suggesting a role for these diverse ubiquitin modifications in synaptic plasticity and memory formation. We conclude by discussing how technological limitations have limited our ability to identify and elucidate the role of different ubiquitin chains in the brain and speculate on the future directions and implications of understanding linkage-specific ubiquitin modifications in activity- and learning-dependent synaptic plasticity.

Indexed as

Neuronal PlasticityProteolysisAnimalsBrainHumansMemoryPolyubiquitinProteasome Endopeptidase ComplexUbiquitinPolyubiquitinProteasome Endopeptidase ComplexUbiquitinMemoryProtein degradationTranscriptionUbiquitin

Identifiers

PMID32745599
PMCPMC7484030

What Socratic 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 Socratic graph.