Evidence map›Paper›PMID 27796752›Full record

ArticleMolecular neurobiology2017

Synaptic ERK2 Phosphorylates and Regulates Metabotropic Glutamate Receptor 1 In Vitro and in Neurons.

Ju Hwan Yang, Li-Min Mao, Eun Sang Choe, John Q Wang

Open access · greenAbstract read
In one paragraph

Article in Molecular neurobiology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing 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

17 citing papers in PubMed, 20 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Metabotropic glutamate receptor trafficking.Molecular and cellular neurosciences · 2018
    Review
  12. Na⁺, K⁺-ATPase Signaling and Bipolar Disorder.International journal of molecular sciences · 2018
    Review
  13. Article
  14. miR-217-casein kinase-2 cross talk regulates ERK activation in ganglioglioma.Journal of molecular medicine (Berlin, Germany) · 2017
    Article
  15. Local substrates of non-receptor tyrosine kinases at synaptic sites in neurons.Sheng li xue bao : [Acta physiologica Sinica] · 2017
    Review
  16. Article
  17. Review
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.

Ju Hwan YangDepartment of Biological Sciences, Pusan National University, Busan, 46241, South Korea.
Li-Min MaoDepartment of Anesthesiology, School of Medicine, University of Missouri-Kansas City, Kansas City, MO, 64108, USA.
Eun Sang ChoeDepartment of Biological Sciences, Pusan National University, Busan, 46241, South Korea. eschoe@pusan.ac.kr.
John Q WangDepartment of Anesthesiology, School of Medicine, University of Missouri-Kansas City, Kansas City, MO, 64108, USA. wangjq@umkc.edu.
Pusan National University · KRUniversity of Missouri–Kansas City · US

Funding

REGULATION OF GENE EXPRESSION IN STRIATAL NEURONSR01MH061469 · NIMH · UNIVERSITY OF MISSOURI KANSAS CITY · PI WANG, QIANG · 2001 to 2024
$7.9M
Metabotropic Glutamate Regulation of Amphetamine ActionR01DA010355 · NIDA · UNIVERSITY OF MISSOURI KANSAS CITY · PI WANG, QIANG · 2003 to 2017
$4.6M
METABOTROPIC GLUTAMATE REGULATION OF AMPHETAMINE ACTIONR29DA010355 · NIDA · UNIVERSITY OF MISSOURI KANSAS CITY · PI WANG, QIANG · 1997 to 2001
$198k
NIDA NIH HHS R01 DA010355NIDA NIH HHS R29 DA010355NIMH NIH HHS R01 MH061469
6 · The paper itself

Abstract

A synaptic pool of extracellular signal-regulated kinases (ERK) controls synaptic transmission, although little is known about its underlying signaling mechanisms. Here, we found that synaptic ERK2 directly binds to postsynaptic metabotropic glutamate receptor 1a (mGluR1a). This binding is direct and the ERK-binding site is located in the intracellular C-terminus (CT) of mGluR1a. Parallel with this binding, ERK2 phosphorylates mGluR1a at a cluster of serine residues in the distal part of mGluR1a-CT. In rat cerebellar neurons, ERK2 interacts with mGluR1a at synaptic sites, and active ERK constitutively phosphorylates mGluR1a under normal conditions. This basal phosphorylation is critical for maintaining adequate surface expression of mGluR1a. ERK is also essential for controlling mGluR1a signaling in triggering distinct postreceptor signaling transduction pathways. In summary, we have demonstrated that mGluR1a is a sufficient substrate of ERK2. ERK that interacts with and phosphorylates mGluR1a is involved in the regulation of the trafficking and signaling of mGluR1.

Indexed as

Amino Acid SequenceAnimalsButadienesCerebellumInositol 1,4,5-TrisphosphateMaleMitogen-Activated Protein Kinase 1NeuronsNitrilesPhosphorylationPhosphoserineProtein BindingRats, WistarReceptors, Metabotropic GlutamateSignal Transductionsrc-Family KinasesButadienesInositol 1,4,5-Trisphosphatemetabotropic glutamate receptor type 1Mitogen-Activated Protein Kinase 1NitrilesPhosphoserineReceptors, Metabotropic Glutamatesrc-Family KinasesU 0126CerebellumG protein-coupled receptorIP3MAPKmGluRPhosphorylationSrc

Identifiers

PMID27796752
PMCPMC5410195
OpenAlexW2540805641

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.