Evidence map›Paper›PMID 24452473›Full record

ArticleMolecular pharmacology2014

Regulation of GluA1 α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor function by protein kinase C at serine-818 and threonine-840.

Meagan A Jenkins, Gordon Wells, Julia Bachman, James P Snyder, Andrew Jenkins, Richard L Huganir, Robert E Oswald, Stephen F Traynelis

Open access · bronzeAbstract read
In one paragraph

Article in Molecular pharmacology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.2field-weighted citation impact, top 25% 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

20 citing papers in PubMed, 28 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Phosphorylation-Dependent Regulation of CaFrontiers in synaptic neuroscience · 2020
    Article
  5. Article
  6. Preferential generation of CaThe Journal of biological chemistry · 2019
    Article
  7. Review
  8. Article
  9. Review
  10. Review
  11. Article
  12. Review
  13. Article
  14. Review
  15. Structural rearrangement of the intracellular domains during AMPA receptor activation.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  16. Article
  17. Review
  18. Regulation of AMPA receptor phosphorylation by the neuropeptide PACAP38.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  19. Dopamine receptors - IUPHAR Review 13.British journal of pharmacology · 2015
    Review
  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

8 authors at 1 institution in 1 country.

Meagan A JenkinsDepartment of Pharmacology (M.A.J., A.J., S.F.T.) and Department of Anesthesiology (A.J.), School of Medicine, and Department of Chemistry (G.W., J.P.S.), Emory University, Atlanta, Georgia; Department of Neuroscience and Howard Hughes Medical Institute, Johns Hopkins University School of Medicine, Baltimore, Maryland (J.B., R.L.H.); and Department of Molecular Medicine, Cornell University, Ithaca, New York (R.E.O.).
Gordon Wells
Julia Bachman
James P Snyder
Andrew Jenkins
Richard L Huganir
Robert E Oswald
Stephen F Traynelis
Howard Hughes Medical Institute · US

Funding

Neuroscience Training ProgramT32EY017203 · NEI · JOHNS HOPKINS UNIVERSITY · PI BERGLES, DWIGHT E · 2005 to 2014
$2.9M
NEI NIH HHS T32 EY017203
6 · The paper itself

Abstract

Three residues within the AMPA (α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid) receptor subunit GluA1 C terminus (Ser818, Ser831, Thr840) can be phosphorylated by Ca(2+)/phospholipid-dependent protein kinase (PKC). Here, we show that PKC phosphorylation of GluA1 Ser818 or Thr840 enhances the weighted mean channel conductance without altering the response time course or agonist potency. These data support the idea that these residues constitute a hyper-regulatory domain for the AMPA receptor. Introduction of phosphomimetic mutations increases conductance only at these three sites within the proximal C terminus, consistent with a structural model with a flexible linker connecting the distal C-terminal domain to the more proximal domain containing a helix bracketed by Ser831 and Thr840. NMR spectra support this model and raise the possibility that phosphorylation can alter the configuration of this domain. Our findings provide insight into the structure and function of the C-terminal domain of GluA1, which controls AMPA receptor function and trafficking during synaptic plasticity in the central nervous system.

Indexed as

AnimalsFemaleHEK293 CellsHippocampusHumansMaleMiceModels, MolecularMutationNeuronsPatch-Clamp TechniquesPhosphorylationPrimary Cell CultureProtein ConformationProtein Kinase CRatsProtein Kinase CReceptors, AMPASerineThreonine

Identifiers

PMID24452473
PMCPMC4014661
OpenAlexW2030271777

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.