Evidence map›Paper›PMID 18305116›Full record

ArticleThe Journal of biological chemistry2008

AKAP79 selectively enhances protein kinase C regulation of GluR1 at a Ca2+-calmodulin-dependent protein kinase II/protein kinase C site.

Steven J Tavalin

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
1.9field-weighted citation impact, top 16% 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

37 citing papers in PubMed, 52 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Phosphorylation-Dependent Regulation of CaFrontiers in synaptic neuroscience · 2020
    Article
  5. Article
  6. Article
  7. Preferential generation of CaThe Journal of biological chemistry · 2019
    Article
  8. Hyperspectral imaging microscopy for measurement of localized second messenger signals in single cells.Proceedings of SPIE--the International Society for Optical Engineering · 2019
    Article
  9. Review
  10. Control of Homeostatic Synaptic Plasticity by AKAP-Anchored Kinase and Phosphatase Regulation of CaThe Journal of neuroscience : the official journal of the Society for Neuroscience · 2018
    Article
  11. Review
  12. Article
  13. Estimating the magnitude of near-membrane PDE4 activity in living cells.American journal of physiology. Cell physiology · 2015
    Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Review
  19. Article
  20. A-kinase anchoring proteins regulate compartmentalized cAMP signaling in airway smooth muscle.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2012
    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

1 author at 1 institution in 1 country.

Steven J TavalinDepartment of Pharmacology, University of Tennessee Health Science Center, Memphis, Tennessee 38163, USA. stavalin@utmem.edu
University of Tennessee Health Science Center · US

Funding

Regulation of Ionotropic Glutamate ReceptorsR01NS046661 · NINDS · UNIVERSITY OF TENNESSEE HEALTH SCI CTR · PI TAVALIN, STEVEN J · 2005 to 2008
$915k
NINDS NIH HHS NS46661NINDS NIH HHS R01 NS046661
6 · The paper itself

Abstract

Enhancement of AMPA receptor activity in response to synaptic plasticity inducing stimuli may arise, in part, through phosphorylation of the GluR1 AMPA receptor subunit at Ser-831. This site is a substrate for both Ca(2+)-calmodulin-dependent protein kinase II (CaMKII) and protein kinase C (PKC). However, neuronal protein levels of CaMKII may exceed those of PKC by an order of magnitude. Thus, it is unclear how PKC could effectively regulate this common target site. The multivalent neuronal scaffold A-kinase-anchoring protein 79 (AKAP79) is known to bind PKC and is linked to GluR1 by synapse-associated protein 97 (SAP97). Here, biochemical studies demonstrate that AKAP79 localizes PKC activity near the receptor, thus accelerating Ser-831 phosphorylation. Complementary electrophysiological studies indicate that AKAP79 selectively shifts the dose-dependence for PKC modulation of GluR1 receptor currents approximately 20-fold, such that low concentrations of PKC are as effective as much higher CaMKII concentrations. By boosting PKC activity near a target substrate, AKAP79 provides a mechanism to overcome limitations in kinase abundance thereby ensuring faithful signal propagation and efficient modification of AMPA receptor-mediated responses.

Indexed as

Gene Expression RegulationA Kinase Anchor ProteinsCalciumCalcium-Calmodulin-Dependent Protein Kinase Type 2Cell LineElectrophysiologyHippocampusHumansModels, BiologicalNeuronsPhosphorylationProtein Kinase CReceptors, AMPATime FactorsAKAP5 protein, humanA Kinase Anchor ProteinsCalciumCalcium-Calmodulin-Dependent Protein Kinase Type 2Protein Kinase CReceptors, AMPA

Identifiers

PMID18305116
PMCPMC2431053
OpenAlexW2068320316

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.