Evidence map›Paper›PMID 25253852›Full record

ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2014

Two protein N-acetylgalactosaminyl transferases regulate synaptic plasticity by activity-dependent regulation of integrin signaling.

Neil Dani, He Zhu, Kendal Broadie

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2014. 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
1.5field-weighted citation impact, top 19% 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

21 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Mucin-TypeFrontiers in neuroanatomy · 2021
    Article
  7. Review
  8. Review
  9. Review
  10. Article
  11. Article
  12. Review
  13. COG7 deficiency inJournal of cell science · 2017
    Article
  14. Article
  15. Activity-Induced Synaptic Structural Modifications by an Activator of Integrin Signaling at theThe Journal of neuroscience : the official journal of the Society for Neuroscience · 2017
    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 2 institutions in 1 country.

Neil DaniDepartments of Biological Sciences, Cell and Developmental Biology, and Pharmacology and The Vanderbilt Kennedy Center for Research on Human Development, Vanderbilt University, Nashville, Tennessee 37232.
He ZhuDepartments of Biological Sciences, Cell and Developmental Biology, and Pharmacology and The Vanderbilt Kennedy Center for Research on Human Development, Vanderbilt University, Nashville, Tennessee 37232.
Kendal BroadieDepartments of Biological Sciences, Cell and Developmental Biology, and Pharmacology and The Vanderbilt Kennedy Center for Research on Human Development, Vanderbilt University, Nashville, Tennessee 37232 kendal.broadie@vanderbilt.edu.
Vanderbilt University · USJohn F. Kennedy Center for the Performing Arts · US

Funding

Genetic Analysis of Synapse Formation and FunctionR01MH096832 · NIMH · VANDERBILT UNIVERSITY · PI BROADIE, KENDAL · 2012 to 2016
$2.3M
NIMH NIH HHS MH096832NIMH NIH HHS R01 MH096832
6 · The paper itself

Abstract

Using a Drosophila whole-genome transgenic RNAi screen for glycogenes regulating synapse function, we have identified two protein α-N-acetylgalactosaminyltransferases (pgant3 and pgant35A) that regulate synaptic O-linked glycosylation (GalNAcα1-O-S/T). Loss of either pgant alone elevates presynaptic/postsynaptic molecular assembly and evoked neurotransmission strength, but synapses appear restored to normal in double mutants. Likewise, activity-dependent facilitation, augmentation, and posttetanic potentiation are all suppressively impaired in pgant mutants. In non-neuronal contexts, pgant function regulates integrin signaling, and we show here that the synaptic Position Specific 2 (αPS2) integrin receptor and transmembrane tenascin ligand are both suppressively downregulated in pgant mutants. Channelrhodopsin-driven activity rapidly (<1 min) drives integrin signaling in wild-type synapses but is suppressively abolished in pgant mutants. Optogenetic stimulation in pgant mutants alters presynaptic vesicle trafficking and postsynaptic pocket size during the perturbed integrin signaling underlying synaptic plasticity defects. Critically, acute blockade of integrin signaling acts synergistically with pgant mutants to eliminate all activity-dependent synaptic plasticity.

Indexed as

Neuronal PlasticityAnimalsDrosophilaDrosophila ProteinsIntegrin alpha ChainsN-AcetylgalactosaminyltransferasesNeuromuscular JunctionSynaptic TransmissionSynaptic VesiclesTenascinDrosophila Proteinsif protein, DrosophilaIntegrin alpha ChainsN-AcetylgalactosaminyltransferasesPgant3 protein, DrosophilaTenascinactivity dependentDrosophilaintegrinneuromuscular junctionO-linked glycosylationplasticity

Identifiers

PMID25253852
PMCPMC4172800
OpenAlexW2087404679

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.