Evidence map›Paper›PMID 23612982›Full record

ArticleThe Journal of biological chemistry2013

Regulation of metabotropic glutamate receptor 7 (mGluR7) internalization and surface expression by Ser/Thr protein phosphatase 1.

Young Ho Suh, Ji-Young Park, Sangwook Park, Ilo Jou, Paul A Roche, Katherine W Roche

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.3field-weighted citation impact, top 24% 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

12 citing papers in PubMed, 30 citations in OpenAlex.

  1. Review
  2. Article
  3. PathogenicThe Journal of neuroscience : the official journal of the Society for Neuroscience · 2021
    Article
  4. Review
  5. Article
  6. Article
  7. Metabotropic glutamate receptor trafficking.Molecular and cellular neurosciences · 2018
    Review
  8. Article
  9. Review
  10. Review
  11. Review
  12. TNF-α downregulates inhibitory neurotransmission through protein phosphatase 1-dependent trafficking of GABA(A) receptors.The Journal of neuroscience : the official journal of the Society for Neuroscience · 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

6 authors at 3 institutions in 2 countries.

Young Ho SuhDepartment of Pharmacology and Chronic Inflammatory Disease Research Center, Ajou University School of Medicine, Suwon 443-721, South Korea. suhy@ajou.ac.kr
Ji-Young Park
Sangwook Park
Ilo Jou
Paul A Roche
Katherine W Roche
Ajou University · KRNational Institutes of Health · USNational Institute of Neurological Disorders and Stroke · US

Funding

Subunit-Specific Regulation Of Glutamate ReceptorsZIANS002994 · NINDS · NATIONAL INSTITUTE OF NEUROLOGICAL DISORDERS AND STROKE · PI ROCHE, KATHERINE · 2009 to 2025
$30.0M
Regulation of Metabotropic Glutamate Receptor SignalingZIANS003036 · NINDS · NATIONAL INSTITUTE OF NEUROLOGICAL DISORDERS AND STROKE · PI ROCHE, KATHERINE · 2009 to 2013
$3.8M
Intramural NIH HHS
6 · The paper itself

Abstract

The metabotropic glutamate receptor type 7 (mGluR7) is the predominant group III mGluR in the presynaptic active zone, where it serves as an autoreceptor to inhibit neurotransmitter release. Our previous studies show that PKC phosphorylation of mGluR7 on Ser-862 is a key mechanism controlling constitutive and activity-dependent surface expression of mGluR7 by regulating a competitive interaction of calmodulin and protein interacting with C kinase (PICK1). As receptor phosphorylation and dephosphorylation are tightly coordinated through the precise action of protein kinases and phosphatases, dephosphorylation by phosphatases is likely to play an active role in governing the activity-dependent or agonist-induced changes in mGluR7 receptor surface expression. In the present study, we find that the serine/threonine protein phosphatase 1 (PP1) has a crucial role in the constitutive and agonist-induced dephosphorylation of Ser-862 on mGluR7. Treatment of neurons with PP1 inhibitors leads to a robust increase in Ser-862 phosphorylation and increased surface expression of mGluR7. In addition, Ser-862 phosphorylation of both mGluR7a and mGluR7b is a target of PP1. Interestingly, agonist-induced dephosphorylation of mGluR7 is regulated by PP1, whereas NMDA-mediated activity-induced dephosphorylation is not, illustrating there are multiple signaling pathways that affect receptor phosphorylation and trafficking. Importantly, PP1γ1 regulates agonist-dependent Ser-862 dephosphorylation and surface expression of mGluR7.

Indexed as

AminobutyratesAnimalsEndocytosisExcitatory Amino Acid AgonistsHEK293 CellsHippocampusHumansNeuronsN-MethylaspartatePhosphorylationPrimary Cell CultureProtein Phosphatase 1Protein Processing, Post-TranslationalProtein TransportRatsRats, Sprague-Dawley2-amino-4-phosphonobutyric acidAminobutyratesExcitatory Amino Acid Agonistsmetabotropic glutamate receptor 7N-MethylaspartateProtein Phosphatase 1Receptors, Metabotropic GlutamateGlutamate Receptor MetabotropicG Protein Coupled Receptors (GPCR)Protein PhosphorylationReceptor EndocytosisSerine Threonine Protein PhosphataseSynapses

Identifiers

PMID23612982
PMCPMC3682553
OpenAlexW2019893507

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.