Evidence map›Paper›PMID 22373567›Full record

ArticleChannels (Austin, Tex.)

PKC phosphorylates GluA1-Ser831 to enhance AMPA receptor conductance.

Meagan A Jenkins, Stephen F Traynelis

Abstract read
In one paragraph

Article in Channels (Austin, Tex.). The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
–field-weighted citation impact
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

35 citing papers in PubMed.

  1. Review
  2. ESCRT-0 regulates AMPA receptor currents and CabioRxiv : the preprint server for biology · 2026
    Article
  3. Review
  4. Review
  5. Review
  6. Article
  7. Review
  8. Article
  9. Article
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  11. Article
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  14. Review
  15. Article
  16. Article
  17. Article
  18. Preferential generation of CaThe Journal of biological chemistry · 2019
    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

2 authors.

Meagan A JenkinsDepartment of Pharmacology, Emory University School of Medicine, Atlanta, GA, USA.
Stephen F Traynelis

Funding

Control of AMPA receptor function by phosphorylationR01NS068464 · NINDS · EMORY UNIVERSITY · PI TRAYNELIS, STEPHEN F · 2010 to 2013
$1.3M
NINDS NIH HHS NS068464NINDS NIH HHS R01 NS068464
6 · The paper itself

Abstract

AMPA receptors mediate fast excitatory synaptic transmission in the brain, and are dynamically regulated by phosphorylation of multiple residues within the C-terminal domain. CaMKII phosphorylates Ser831 within the AMPA receptor GluA1 subunit to increase single channel conductance, and biochemical studies show that PKC can also phosphorylate this residue. In light of the discovery of additional PKC phosphorylation sites within the GluA1 C-terminus, it remains unclear whether PKC phosphorylation of Ser831 increases GluA1 conductance in intact receptors. Here, we report that the purified, catalytic subunit of PKC significantly increases the conductance of wild-type GluA1 AMPA receptors expressed in the presence of stargazin in HEK293T cells. Furthermore, the mutation GluA1-S831A blocks the functional effect of PKC. These findings suggest that GluA1 AMPA receptor conductance can be increased by activated CaMKII or PKC, and that phosphorylation at this site provides a mechanism for channel modulation via a variety of protein signaling cascades.

Indexed as

AnimalsCalcium-Calmodulin-Dependent Protein Kinase Type 2HEK293 CellsHumansPhosphorylationProtein Kinase CProtein SubunitsRatsReceptors, AMPACalcium-Calmodulin-Dependent Protein Kinase Type 2Protein Kinase CProtein SubunitsReceptors, AMPAAMPA receptorGluA1GluR1phosphorylationPKC

Identifiers

PMID22373567
PMCPMC3367675

What OpenQuestion holds

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Registered trials

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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.