Evidence map›Paper›PMID 25639954›Full record

ArticleJournal of neurochemistry2015

Protein kinase A directly phosphorylates metabotropic glutamate receptor 5 to modulate its function.

Ken Uematsu, Myriam Heiman, Marina Zelenina, Júlio Padovan, Brian T Chait, Anita Aperia, Akinori Nishi, Paul Greengard

Abstract read
In one paragraph

Article in Journal of neurochemistry, 2015. 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
1.4field-weighted citation impact, top 21% 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, 31 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Review
  10. Review
  11. Activated CaMKIIMolecular pharmacology · 2018
    Article
  12. Metabotropic glutamate receptor trafficking.Molecular and cellular neurosciences · 2018
    Review
  13. Review
  14. Article
  15. Review
  16. 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

8 authors at 4 institutions in 3 countries.

Ken UematsuLaboratory of Molecular and Cellular Neuroscience, The Rockefeller University, New York, New York, USA; Department of Pharmacology, Kurume University School of Medicine, Kurume, Fukuoka, Japan; Department of Psychiatry, Kurume University School of Medicine, Kurume, Fukuoka, Japan; Cognitive and Molecular Research Institute of Brain Diseases, Kurume University, Kurume, Fukuoka, Japan.
Myriam Heiman
Marina Zelenina
Júlio Padovan
Brian T Chait
Anita Aperia
Akinori Nishi
Paul Greengard
Rockefeller University · USKarolinska Institutet · SEKTH Royal Institute of Technology · SEKurume University · JP

Funding

THE ROLE OF DARPPS IN THE ACUTE AND CHRONIC EFFECTS OF COCAINE AND AMPHETAMINEP01DA010044 · NIDA · ROCKEFELLER UNIVERSITY · PI GREENGARD, PAUL · 1996 to 2015
$23.6M
National Resource for Mass Spectrom of Biological MacromoleculesP41GM103314 · NIGMS · ROCKEFELLER UNIVERSITY · PI CHAIT, BRIAN T · 2012 to 2017
$9.9M
Striatal Cell-specific Analysis of the Molecular Mechanisms of Antipsychotic DrugP50MH090963 · NIMH · ROCKEFELLER UNIVERSITY · PI GREENGARD, PAUL · 2010 to 2014
$9.8M
NIDA NIH HHS DA10044NIDA NIH HHS P01 DA010044NIGMS NIH HHS P41 GM103314NIMH NIH HHS MH090963NIMH NIH HHS P50 MH090963
6 · The paper itself

Abstract

Metabotropic glutamate receptor 5 (mGluR5) regulates excitatory post-synaptic signaling in the central nervous system (CNS) and is implicated in various CNS disorders. Protein kinase A (PKA) signaling is known to play a critical role in neuropsychiatric disorders such as Parkinson's disease, schizophrenia, and addiction. Dopamine signaling is known to modulate the properties of mGluR5 in a cAMP- and PKA-dependent manner, suggesting that mGluR5 may be a direct target for PKA. Our study identifies mGluR5 at Ser870 as a direct substrate for PKA phosphorylation and demonstrates that this phosphorylation plays a critical role in the PKA-mediated modulation of mGluR5 functions such as extracellular signal-regulated kinase phosphorylation and intracellular Ca(2+) oscillations. The identification of the molecular mechanism by which PKA signaling modulates mGluR5-mediated cellular responses contributes to the understanding of the interaction between dopaminergic and glutamatergic neuronal signaling. We identified serine residue 870 (S870) in metabotropic glutamate receptor 5 (mGluR5) as a direct substrate for protein kinase A (PKA). The phosphorylation of this site regulates the ability of mGluR5 to induce extracellular signal-regulated kinase (ERK) phosphorylation and intracellular Ca(2+) oscillations. This study provides a direct molecular mechanism by which PKA signaling interacts with glutamate neurotransmission.

Indexed as

Amino Acid SequenceAnimalsBinding SitesCyclic AMP-Dependent Protein KinasesHEK293 CellsHumansMiceMice, Inbred C57BLMice, KnockoutOrgan Culture TechniquesPhosphorylationReceptor, Metabotropic Glutamate 5Cyclic AMP-Dependent Protein KinasesReceptor, Metabotropic Glutamate 5Ca2+ oscillationsextracellular signal-regulated kinasemGluR5phosphorylationprotein kinase A

Identifiers

PMID25639954
PMCPMC4359654
OpenAlexW2105706450

What OpenQuestion holds

Textmetadata
LicenceTDM
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.