Evidence map›Paper›PMID 11739572›Full record

ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2001

Metabotropic glutamate receptor 5-induced phosphorylation of extracellular signal-regulated kinase in astrocytes depends on transactivation of the epidermal growth factor receptor.

R D Peavy, M S Chang, E Sanders-Bush, P J Conn

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

40 citing papers in PubMed, 107 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Review
  6. Review
  7. Article
  8. Article
  9. A role for the purinergic receptor P2XScientific reports · 2017
    Article
  10. Noise Stress Induces an Epidermal Growth Factor Receptor/Xeroderma Pigmentosum-A Response in the Auditory Nerve.The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society · 2017
    Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. 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 1 country.

R D PeavyDepartment of Pharmacology, Emory University School of Medicine and Graduate Program in Molecular and Systems Pharmacology, Graduate Division of Biological and Biomedical Sciences, Emory University, Atlanta, Georgia 30322, USA.
M S Chang
E Sanders-Bush
P J Conn
Emory University · USVanderbilt University · US

Funding

NIMH NIH HHS MH12398NIMH NIH HHS MH34001
6 · The paper itself

Abstract

G-protein-coupled receptors (GPCRs) induce the phosphorylation of mitogen-activated protein (MAP) kinase by actions on any of a number of signal transduction systems. Previous studies have revealed that activation of the G(q)-coupled metabotropic glutamate receptor 5 (mGluR5) induces phosphorylation of the MAP kinase extracellular signal-regulated kinase 2 (ERK2) in cultured rat cortical astrocytes. We performed a series of studies to determine the mechanisms underlying mGluR5-induced phosphorylation of MAP kinase in these cells. Interestingly, our studies suggest that mGluR5-mediated ERK2 phosphorylation is dependent on the activation of G(alphaq) but is not mediated by the activation of phospholipase Cbeta1, activation of protein kinase C, or increases in intracellular calcium. Studies with peptide inhibitors suggest that this response is not dependent on G(betagamma) subunits. However, the activation of ERK2 was dependent on activation of the epidermal growth factor (EGF) receptor and activation of a Src family tyrosine kinase. Furthermore, activation of mGluR5 induced an association of this receptor and the EGF receptor, suggesting the formation of a signaling complex involved in the activation of ERK2. These data suggest that mGluR5 increases ERK2 phosphorylation in astrocytes by a novel mechanism involving the activation of G(alphaq) and both receptor and nonreceptor tyrosine kinases but that is independent of the activation of phospholipase Cbeta1.

Indexed as

AnimalsAstrocytesCells, CulturedEnzyme InhibitorsErbB ReceptorsExcitatory Amino Acid AgonistsExcitatory Amino Acid AntagonistsGTP-Binding Protein alpha Subunits, Gq-G11GTP-Binding ProteinsHeterotrimeric GTP-Binding ProteinsIsoenzymesMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3Mitogen-Activated Protein KinasesPeptidesPhosphatidylinositolsEnzyme InhibitorsErbB ReceptorsExcitatory Amino Acid AgonistsExcitatory Amino Acid AntagonistsGrm5 protein, ratGTP-Binding Protein alpha Subunits, Gq-G11GTP-Binding ProteinsHeterotrimeric GTP-Binding ProteinsIsoenzymesMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3Mitogen-Activated Protein KinasesPeptidesPhosphatidylinositolsPhospholipase C betaProtein SubunitsProtein Tyrosine PhosphatasesQuinazolinesReceptor, Metabotropic Glutamate 5Receptors, Metabotropic GlutamateRTKI cpdsrc-Family KinasesType C PhospholipasesTyrphostins

Identifiers

PMID11739572
PMCPMC6763045
OpenAlexW2101415694

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.