Evidence map›Paper›PMID 23035237›Full record

ArticleMolecular & cellular proteomics : MCP2013

Activity-dependent protein dynamics define interconnected cores of co-regulated postsynaptic proteins.

Jonathan C Trinidad, Agnes Thalhammer, Alma L Burlingame, Ralf Schoepfer

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.1field-weighted citation impact, top 27% 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

16 citing papers in PubMed, 25 citations in OpenAlex.

  1. Article
  2. Regulatory mechanisms in postsynaptic phosphorylation networks.Current opinion in structural biology · 2019
    Review
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Review
  9. Glial Contributions to Neural Function and Disease.Molecular & cellular proteomics : MCP · 2016
    Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. Recent advances in quantitative neuroproteomics.Methods (San Diego, Calif.) · 2013
    Review
  16. Proteomic analysis of postsynaptic density in Alzheimer's disease.Clinica chimica acta; international journal of clinical chemistry · 2013
    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 2 institutions in 2 countries.

Jonathan C TrinidadMass Spectrometry Facility, Department of Pharmaceutical Chemistry, University of California, San Francisco, California 94158-2517, USA.
Agnes Thalhammer
Alma L Burlingame
Ralf Schoepfer
University College London · GBUniversity of California, San Francisco · US

Funding

Rewiring Therapeutic Cells: User-Controlled T Cells and Stem CellsP50GM081879 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI LIM, WENDELL A · 2010 to 2017
$19.0M
Bio-Organic Biomedical Mass Spectromy ResourceP41GM103481 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI BURLINGAME, ALMA L · 2012 to 2015
$6.4M
Biotechnology and Biological Sciences Research CouncilNIGMS NIH HHS 8P41GM103481NIGMS NIH HHS P41 GM103481NIGMS NIH HHS P50 GM081879Wellcome Trust
6 · The paper itself

Abstract

Synapses are highly dynamic structures that mediate cell-cell communication in the central nervous system. Their molecular composition is altered in an activity-dependent fashion, which modulates the efficacy of subsequent synaptic transmission events. Whereas activity-dependent trafficking of individual key synaptic proteins into and out of the synapse has been characterized previously, global activity-dependent changes in the synaptic proteome have not been studied. To test the feasibility of carrying out an unbiased large-scale approach, we investigated alterations in the molecular composition of synaptic spines following mass stimulation of the central nervous system induced by pilocarpine. We observed widespread changes in relative synaptic abundances encompassing essentially all proteins, supporting the view that the molecular composition of the postsynaptic density is tightly regulated. In most cases, we observed that members of gene families displayed coordinate regulation even when they were not known to physically interact. Analysis of correlated synaptic localization revealed a tightly co-regulated cluster of proteins, consisting of mainly glutamate receptors and their adaptors. This cluster constitutes a functional core of the postsynaptic machinery, and changes in its size affect synaptic strength and synaptic size. Our data show that the unbiased investigation of activity-dependent signaling of the postsynaptic density proteome can offer valuable new information on synaptic plasticity.

Indexed as

Synaptic TransmissionAnimalsCell CommunicationCell MembraneCentral Nervous SystemDisks Large Homolog 4 ProteinGuanylate KinasesMaleMembrane ProteinsMiceMice, Inbred C57BLNeuronal PlasticityNeuronsPilocarpinePost-Synaptic DensityProtein TransportDisks Large Homolog 4 ProteinDlg4 protein, mouseGuanylate KinasesMembrane ProteinsPilocarpineReceptors, Glutamate

Identifiers

PMID23035237
PMCPMC3536907
OpenAlexW2018093424

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.