Evidence map›Paper›PMID 26915533›Full record

ReviewThe Journal of physiology2016

Bassoon and piccolo regulate ubiquitination and link presynaptic molecular dynamics with activity-regulated gene expression.

Daniela Ivanova, Anika Dirks, Anna Fejtova

Open access · greenAbstract readReview
In one paragraph

Review in The Journal of physiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.8field-weighted citation impact, top 11% 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

23 citing papers in PubMed, 36 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Molecular Physiology of the Neuronal Synapse.Current issues in molecular biology · 2026
    Review
  5. Review
  6. Article
  7. Article
  8. Behavioral and histological analyses of the mouseFrontiers in neuroscience · 2024
    Article
  9. Article
  10. Article
  11. Article
  12. CBeLife · 2020
    Article
  13. Article
  14. Review
  15. A Multiple Piccolino-RIBEYE Interaction Supports Plate-Shaped Synaptic Ribbons in Retinal Neurons.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2019
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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

3 authors at 1 institution in 1 country.

Daniela IvanovaRG Presynaptic Plasticity, Leibniz Institute for Neurobiology, Magdeburg, Germany.
Anika DirksDepartment of Neurochemistry and Molecular Biology, Leibniz Institute for Neurobiology, Magdeburg, Germany.
Anna FejtovaRG Presynaptic Plasticity, Leibniz Institute for Neurobiology, Magdeburg, Germany. afejtova@lin-magdeburg.de.
Leibniz Institute for Neurobiology · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Release of neurotransmitter is executed by complex multiprotein machinery, which is assembled around the presynaptic cytomatrix at the active zone. One well-established function of this proteinaceous scaffold is the spatial organization of synaptic vesicle cluster, the protein complexes that execute membrane fusion and compensatory endocytosis, and the transmembrane molecules important for alignment of pre- and postsynaptic structures. The presynaptic cytomatrix proteins function also in processes other than the formation of a static frame for assembly of the release apparatus and synaptic vesicle cycling. They actively contribute to the regulation of multiple steps in this process and are themselves an important subject of regulation during neuronal plasticity. We are only beginning to understand the mechanisms and signalling pathways controlling these regulations. They are mainly dependent on posttranslational modifications, including phosphorylation and small-molecules conjugation, such as ubiquitination. Ubiquitination of presynaptic proteins might lead to their degradation by proteasomes, but evidence is growing that this modification also affects their function independently of their degradation. Signalling from presynapse to nucleus, which works on a much slower time scale and more globally, emerged as an important mechanism for persistent usage-dependent and homeostatic neuronal plasticity. Recently, two new functions for the largest presynaptic scaffolding proteins bassoon and piccolo emerged. They were implied (1) in the regulation of specific protein ubiquitination and proteasome-mediated proteolysis that potentially contributes to short-term plasticity at the presynapse and (2) in the coupling of activity-induced molecular rearrangements at the presynapse with reprogramming of expression of neuronal activity-regulated genes.

Indexed as

Gene Expression RegulationAlcohol OxidoreductasesAnimalsBrain DiseasesCytoskeletal ProteinsDNA-Binding ProteinsMolecular Dynamics SimulationNerve Tissue ProteinsNeuropeptidesNeurotransmitter AgentsSynapsesUbiquitinationAlcohol OxidoreductasesBsn protein, mouseC-terminal binding proteinCytoskeletal ProteinsDNA-Binding ProteinsNerve Tissue ProteinsNeuropeptidesNeurotransmitter AgentsPclo protein, mouse

Identifiers

PMID26915533
PMCPMC5043050
OpenAlexW2284057097

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.