Evidence map›Paper›PMID 27488904›Full record

ArticleScientific reports2016

PACSIN1 regulates the dynamics of AMPA receptor trafficking.

Jocelyn Widagdo, Huaqiang Fang, Se Eun Jang, Victor Anggono

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

34 citing papers in PubMed, 50 citations in OpenAlex.

  1. Article
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  5. Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. Familial ALS-associatedOpen biology · 2022
    Article
  11. Article
  12. PACSIN proteins in vivo: Roles in development and physiology.Acta physiologica (Oxford, England) · 2022
    Review
  13. Article
  14. Regulation of Synapse Weakening through Interactions of the Microtubule Associated Protein Tau with PACSIN1.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2021
    Article
  15. Article
  16. Article
  17. Article
  18. A Novel Glycine Receptor Variant with Startle Disease Affects Syndapin I and Glycinergic Inhibition.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2020
    Article
  19. Palmitoylated Proteins in Dendritic Spine Remodeling.Frontiers in synaptic neuroscience · 2020
    Article
  20. Article
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

4 authors at 3 institutions in 2 countries.

Jocelyn WidagdoClem Jones Centre for Ageing Dementia Research, Queensland Brain Institute, The University of Queensland, Brisbane, QLD 4072, Australia.
Huaqiang FangSolomon H. Snyder Department of Neuroscience, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.
Se Eun JangClem Jones Centre for Ageing Dementia Research, Queensland Brain Institute, The University of Queensland, Brisbane, QLD 4072, Australia.
Victor AnggonoClem Jones Centre for Ageing Dementia Research, Queensland Brain Institute, The University of Queensland, Brisbane, QLD 4072, Australia.
Park Centre for Mental Health · AUJohns Hopkins Medicine · USUniversity of Queensland · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Dynamic trafficking of AMPA receptors (AMPARs) into and out of synapses plays an important role in synaptic plasticity. We previously reported that the protein kinase C and casein kinase II substrate in neurons (PACSIN) forms a complex with AMPARs through its interaction with the protein interacting with C-kinase 1 (PICK1) to regulate NMDA receptor (NMDAR)-induced AMPAR endocytosis and cerebellar long-term depression. However, the molecular mechanism by which PACSIN regulates the dynamics of AMPAR trafficking remains unclear. Using a pH-sensitive green fluorescent protein, pHluorin, tagged to the extracellular domain of the GluA2 subunit of AMPARs, we demonstrate dual roles for PACSIN1 in controlling the internalization and recycling of GluA2 after NMDAR activation. Structure and function analysis reveals a requirement for the PACSIN1 F-BAR and SH3 domains in controlling these NMDAR-dependent processes. Interestingly, the variable region, which binds to PICK1, is not essential for NMDAR-dependent GluA2 internalization and is required only for the correct recycling of AMPARs. These results indicate that PACSIN is a versatile membrane deformation protein that links the endocytic and recycling machineries essential for dynamic AMPAR trafficking in neurons.

Indexed as

Adaptor Proteins, Signal TransducingAnimalsCarrier ProteinsCell Cycle ProteinsCells, CulturedCytoskeletal ProteinsEndocytosisGene Knockdown TechniquesGreen Fluorescent ProteinsIntracellular Signaling Peptides and ProteinsMiceMice, KnockoutModels, NeurologicalNeuronsNeuropeptidesNuclear ProteinsAdaptor Proteins, Signal TransducingCarrier ProteinsCell Cycle ProteinsCytoskeletal Proteinsglutamate receptor ionotropic, AMPA 2Green Fluorescent ProteinsIntracellular Signaling Peptides and ProteinsNeuropeptidesNuclear ProteinsPacsin1 protein, mousePacsin1 protein, ratPHluorinPhosphoproteinsPrkcabp protein, mouseReceptors, AMPAReceptors, N-Methyl-D-Aspartate

Identifiers

PMID27488904
PMCPMC4973260
OpenAlexW2487849081

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.