Evidence map›Paper›PMID 12151513›Full record

ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2002

Receptor for activated C kinase-1 facilitates protein kinase C-dependent phosphorylation and functional modulation of GABA(A) receptors with the activation of G-protein-coupled receptors.

Nicholas J Brandon, Jasmina N Jovanovic, Trevor G Smart, Stephen J Moss

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

49 citing papers in PubMed, 103 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Article
  5. Article
  6. Review
  7. Regulation of CaPflugers Archiv : European journal of physiology · 2022
    Article
  8. Article
  9. Significance of GABAInternational journal of molecular sciences · 2021
    Review
  10. Article
  11. Temporal dynamics of learning-promoted synaptic diversity in CA1 pyramidal neurons.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019
    Article
  12. Feature Article: Selective modulation of tonically active GABAExperimental biology and medicine (Maywood, N.J.) · 2018
    Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Regulation of GABAARs by phosphorylation.Advances in pharmacology (San Diego, Calif.) · 2015
    Review
  18. Review
  19. Article
  20. Neurosteroids promote phosphorylation and membrane insertion of extrasynaptic GABAA receptors.Proceedings of the National Academy of Sciences of the United States of America · 2014
    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.

Nicholas J BrandonMedical Research Council, Laboratory of Molecular Cell Biology and Department of Pharmacology, University College London, London WC1E 6BT, United Kingdom.
Jasmina N Jovanovic
Trevor G Smart
Stephen J Moss
MRC Laboratory for Molecular Cell Biology · GBMedical Research Council · GB

Funding

Wellcome Trust
6 · The paper itself

Abstract

GABA(A) receptors are the principal sites of fast synaptic inhibition in the brain. These receptors are hetero-pentamers that can be assembled from a number of subunit classes: alpha(1-6), beta(1-3), gamma(1-3), delta(1), epsilon, theta;, and pi, but the majority of receptor subtypes is believed, however, to be composed of alpha, beta, and gamma2 subunits. A major mechanism for modulating GABA(A) receptor function occurs via the phosphorylation of residues within the intracellular domains of receptor subunits by a range of serine/threonine and tyrosine kinases. However, how protein kinases are targeted to these receptors to facilitate functional modulation remains unknown. Here we demonstrate that the receptor for activated C kinase (RACK-1) and protein kinase C (PKC) bind to distinct sites on GABA(A) receptor beta subunits. Although RACK-1 is not essential for PKC binding to GABA(A) receptor beta subunits, it enhances the phosphorylation of serine 409, a residue critical for the phospho-dependent modulation of GABA(A) receptor function in the beta1 subunit by anchored PKC. Furthermore, RACK-1 also enhances GABA(A) receptor functional modulation in neurons by a PKC-dependent signaling pathway with the activation of muscarinic acetylcholine receptors (mAChRs). This PKC-dependent modulation of neuronal GABA(A) receptors was mirrored by an increase in the phosphorylation of GABA(A) receptor beta subunits with the activation of mAChRs. Our results suggest a central role for RACK-1 in potentiating PKC-dependent phosphorylation and functional modulation of GABA(A) receptors. Therefore, RACK-1 will enhance functional cross talk between GABA(A) receptors and G-protein-coupled receptors and therefore may have profound effects on neuronal excitability.

Indexed as

Protein SubunitsAnimalsBinding SitesCells, CulturedGTP-Binding ProteinsHumansIsoenzymesKidneyMacromolecular SubstancesNeuronsPhosphorylationProtein BindingProtein Kinase CProtein Structure, TertiaryRatsRats, Sprague-DawleyGTP-Binding ProteinsIsoenzymesMacromolecular SubstancesProtein Kinase CProtein SubunitsReceptors, Cell SurfaceReceptors for Activated C KinaseReceptors, GABA-AReceptors, Muscarinic

Identifiers

PMID12151513
PMCPMC6758144
OpenAlexW2170136226

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.