Evidence map›Paper›PMID 36073248›Full record

ReviewActa physiologica (Oxford, England)2022

Molecular physiology of Arc/Arg3.1: The oligomeric state hypothesis of synaptic plasticity.

Maria Steene Eriksen, Clive R Bramham

Open access · hybridAbstract readReview
In one paragraph

Review in Acta physiologica (Oxford, England), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.7field-weighted citation impact, top 9% 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

19 citing papers in PubMed, 28 citations in OpenAlex.

  1. Nanoscale Spatial Organization of ARC High- and Low-Order Assemblies at Excitatory Synapses.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  2. Article
  3. Article
  4. Article
  5. "Arc - A viral vector of memory and synaptic plasticity".Current opinion in neurobiology · 2025
    Review
  6. Article
  7. Review
  8. Review
  9. Developing forebrain synapses are uniquely vulnerable to sleep loss.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  10. Article
  11. Analysis of Arc/Arg3.1 Oligomerization In Vitro and in Living Cells.International journal of molecular sciences · 2024
    Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
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.

Maria Steene EriksenDepartment of Biomedicine, University of Bergen, Bergen, Norway.
Clive R BramhamDepartment of Biomedicine, University of Bergen, Bergen, Norway.ORCID 0000-0001-5958-7115
University of Bergen · NO

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The immediate early gene, Arc, is a pivotal regulator of synaptic plasticity, memory, and cognitive flexibility. But what is Arc protein? How does it work? Inside the neuron, Arc is a protein interaction hub and dynamic regulator of intra-cellular signaling in synaptic plasticity. In remarkable contrast, Arc can also self-assemble into retrovirus-like capsids that are released in extracellular vesicles and capable of intercellular transfer of RNA. Elucidation of the molecular basis of Arc hub and capsid functions, and the relationship between them, is vital for progress. Here, we discuss recent findings on Arc structure-function and regulation of oligomerization that are giving insight into the molecular physiology of Arc. The unique features of mammalian Arc are emphasized, while drawing comparisons with Drosophila Arc and retroviral Gag. The Arc N-terminal domain, found only in mammals, is proposed to play a key role in regulating Arc hub signaling, oligomerization, and formation of capsids. Bringing together several lines of evidence, we hypothesize that Arc function in synaptic plasticity-long-term potentiation (LTP) and long-term depression (LTD)-are dictated by different oligomeric forms of Arc. Specifically, monomer/dimer function in LTP, tetramer function in basic LTD, and 32-unit oligomer function in enhanced LTD. The role of mammalian Arc capsids is unclear but likely depends on the cross-section of captured neuronal activity-induced RNAs. As the functional states of Arc are revealed, it may be possible to selectively manipulate specific forms of Arc-dependent plasticity and intercellular communication involved in brain function and dysfunction.

Indexed as

Cytoskeletal ProteinsNerve Tissue ProteinsAnimalsLong-Term PotentiationMammalsNeuronal PlasticityRNACytoskeletal ProteinsNerve Tissue ProteinsRNAactivity-regulated cytoskeleton-associated protein (Arc)Gag proteinmemory and cognitionoligomerizationprotein interaction hubprotein structure-functionretrovirus-like capsidsynaptic plasticity

Identifiers

PMID36073248
PMCPMC9787330
OpenAlexW4294991060

What Socratic holds

Textmetadata
LicenceCC BY-NC-ND
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 Socratic graph.