Evidence map›Paper›PMID 23934328›Full record

ReviewNeuromolecular medicine2013

Receptor trafficking and the regulation of synaptic plasticity by SUMO.

Jia Luo, Emi Ashikaga, Philip P Rubin, Michaela J Heimann, Keri L Hildick, Paul Bishop, Fatima Girach, Fernando Josa-Prado, Leo T H Tang, Ruth E Carmichael and 2 more

Abstract readReview
PubMed Publisher
In one paragraph

Review in Neuromolecular medicine, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

24 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
  2. SUMOtherapeutics for Ischemic Stroke.Pharmaceuticals (Basel, Switzerland) · 2023
    Review
  3. Article
  4. Review
  5. Review
  6. Review
  7. Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Commentary: Analysis of SUMO1-conjugation at synapses.Frontiers in cellular neuroscience · 2017
    Article
  14. Article
  15. Article
  16. Sumoylation in Synaptic Function and Dysfunction.Frontiers in synaptic neuroscience · 2016
    Review
  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

12 authors at 1 institution in 1 country.

Jia LuoSchool of Biochemistry, Medical Sciences Building, University of Bristol, University Walk, Bristol, BS8 1TD, UK.
Emi Ashikaga
Philip P Rubin
Michaela J Heimann
Keri L Hildick
Paul Bishop
Fatima Girach
Fernando Josa-Prado
Leo T H Tang
Ruth E Carmichael
Jeremy M Henley
Kevin A Wilkinson
University of Bristol · GB

Funding

Biotechnology and Biological Sciences Research Council BB/K014358/1
6 · The paper itself

Abstract

Timely and efficient information transfer at synapses is fundamental to brain function. Synapses are highly dynamic structures that exhibit long-lasting activity-dependent alterations to their structure and transmission efficiency, a phenomenon termed synaptic plasticity. These changes, which occur through alterations in presynaptic release or in the trafficking of postsynaptic receptor proteins, underpin the formation and stabilisation of neural circuits during brain development, and encode, process and store information essential for learning, memory and cognition. In recent years, it has emerged that the ubiquitin-like posttranslational modification SUMOylation is an important mediator of several aspects of neuronal and synaptic function. Through orchestrating synapse formation, presynaptic release and the trafficking of postsynaptic receptor proteins during forms of synaptic plasticity such as long-term potentiation, long-term depression and homeostatic scaling, SUMOylation is being increasingly appreciated to play a central role in neurotransmission. In this review, we outline key discoveries in this relatively new field, provide an update on recent progress regarding the targets and consequences of protein SUMOylation in synaptic function and plasticity, and highlight key outstanding questions regarding the roles of protein SUMOylation in the brain.

Indexed as

Neuronal PlasticityAnimalsGlycogen Synthase Kinase 3Glycogen Synthase Kinase 3 betaGuanylate KinasesHumansKainic Acid ReceptorsMEF2 Transcription FactorsNerve Tissue ProteinsNeurogenesisNeuronsPotassium ChannelsProtein TransportPTEN PhosphohydrolaseReceptor, Cannabinoid, CB1Receptors, Metabotropic GlutamateCASK kinasesGlycogen Synthase Kinase 3Glycogen Synthase Kinase 3 betaGuanylate KinasesKainic Acid ReceptorsMEF2 Transcription FactorsNerve Tissue ProteinsPotassium ChannelsPTEN PhosphohydrolaseReceptor, Cannabinoid, CB1Receptors, Metabotropic GlutamateReceptors, NeurotransmitterReceptors, PresynapticSmall Ubiquitin-Related Modifier ProteinsUbiquitin-Protein Ligase Complexes

Identifiers

PMID23934328
OpenAlexW1968162971

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.