Evidence map›Paper›PMID 32912969›Full record

ArticleMolecular & cellular proteomics : MCP2020

Temporal Quantitative Proteomics of mGluR-induced Protein Translation and Phosphorylation in Neurons.

Charlotte A G H van Gelder, Renske Penning, Tim S Veth, Lisa A E Catsburg, Casper C Hoogenraad, Harold D MacGillavry, Maarten Altelaar

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.2field-weighted citation impact, top 23% 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

10 citing papers in PubMed, 17 citations in OpenAlex.

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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

7 authors at 2 institutions in 1 country.

Charlotte A G H van GelderBiomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research, and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Utrecht, The Netherlands; Netherlands Proteomics Center, Utrecht, The Netherlands.
Renske PenningBiomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research, and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Utrecht, The Netherlands; Netherlands Proteomics Center, Utrecht, The Netherlands.
Tim S VethBiomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research, and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Utrecht, The Netherlands; Netherlands Proteomics Center, Utrecht, The Netherlands.
Lisa A E CatsburgCell Biology, Department of Biology, Faculty of Science, Utrecht University, Utrecht, The Netherlands.
Casper C HoogenraadCell Biology, Department of Biology, Faculty of Science, Utrecht University, Utrecht, The Netherlands.
Harold D MacGillavryCell Biology, Department of Biology, Faculty of Science, Utrecht University, Utrecht, The Netherlands. Electronic address: H.D.MacGillavry@uu.nl.
Maarten AltelaarBiomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research, and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Utrecht, The Netherlands; Netherlands Proteomics Center, Utrecht, The Netherlands. Electronic address: M.Altelaar@uu.nl.
Utrecht University · NLUniversity of Applied Sciences Utrecht · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

At neuronal synapses, activation of group I metabotropic glutamate receptors (mGluR1/5) triggers a form of long-term depression (mGluR-LTD) that relies on new protein synthesis and the internalization of AMPA-type glutamate receptors. Dysregulation of these processes has been implicated in the development of mental disorders such as autism spectrum disorders and therefore merit a better understanding on a molecular level. Here, to study mGluR-induced signaling pathways, we integrated quantitative phosphoproteomics with the analyses of newly synthesized proteins via bio-orthogonal amino acids (azidohomoalanine) in a pulsed labeling strategy in cultured hippocampal neurons stimulated with DHPG, a specific agonist for group I mGluRs. We identified several kinases with important roles in DHPG-induced mGluR activation, which we confirmed using small molecule kinase inhibitors. Furthermore, changes in the AMPA receptor endocytosis pathway in both protein synthesis and protein phosphorylation were identified, whereby Intersectin-1 was validated as a novel player in this pathway. This study revealed several new insights into the molecular pathways downstream of group I mGluR activation in hippocampal neurons, and provides a rich resource for further analyses.

Indexed as

Protein BiosynthesisProteomicsAmino Acid SequenceAnimalsEndocytosisHippocampusMethoxyhydroxyphenylglycolNeuronsPhosphorylationRatsReceptors, AMPAReceptors, Metabotropic GlutamateSignal TransductionTime Factors3,4-dihydroxyphenylglycolMethoxyhydroxyphenylglycolReceptors, AMPAReceptors, Metabotropic GlutamateAMPA receptormGluR-LTDneurobiologyphosphoproteomeProtein synthesisquantificationsynaptic plasticitytandem mass tagstargeted mass spectrometrytranslation

Identifiers

PMID32912969
PMCPMC7710149
OpenAlexW3084878849

What Socratic 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 Socratic graph.