Evidence map›Paper›PMID 15306641›Full record

ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2004

GABAA receptor phospho-dependent modulation is regulated by phospholipase C-related inactive protein type 1, a novel protein phosphatase 1 anchoring protein.

Miho Terunuma, Il-Sung Jang, Sang Hoon Ha, Josef T Kittler, Takashi Kanematsu, Jasmina N Jovanovic, Keiichi I Nakayama, Norio Akaike, Sung Ho Ryu, Stephen J Moss and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing 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

46 citing papers in PubMed, 106 citations in OpenAlex.

  1. Article
  2. Proteostasis regulation of GABABiomedicine & pharmacotherapy = Biomedecine & pharmacotherapie · 2025
    Review
  3. Article
  4. Article
  5. Article
  6. Anterograde trafficking signals in GABAChannels (Austin, Tex.) · 2019
    Article
  7. Article
  8. Review
  9. Review
  10. Article
  11. γ2 GABAFrontiers in cellular neuroscience · 2018
    Review
  12. General anesthetic actions on GABAJournal of anesthesia · 2017
    Article
  13. Article
  14. Article
  15. Review
  16. Review
  17. Article
  18. Regulation of GABAARs by phosphorylation.Advances in pharmacology (San Diego, Calif.) · 2015
    Review
  19. 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

11 authors at 5 institutions in 5 countries.

Miho TerunumaLaboratory of Molecular and Cellular Biochemistry, Faculty of Dental Science and Station for Collaborative Research, Kyushu University, Fukuoka 812-8582, Japan.
Il-Sung Jang
Sang Hoon Ha
Josef T Kittler
Takashi Kanematsu
Jasmina N Jovanovic
Keiichi I Nakayama
Norio Akaike
Sung Ho Ryu
Stephen J Moss
Masato Hirata
Kyushu University · JPCollaborative Research Group · AUMedical Research Council · GBPohang University of Science and Technology · KRUniversity of Pennsylvania · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

GABA(A) receptors are critical in controlling neuronal activity. Here, we examined the role for phospholipase C-related inactive protein type 1 (PRIP-1), which binds and inactivates protein phosphatase 1alpha (PP1alpha) in facilitating GABA(A) receptor phospho-dependent regulation using PRIP-1-/- mice. In wild-type animals, robust phosphorylation and functional modulation of GABA(A) receptors containing beta3 subunits by cAMP-dependent protein kinase was evident, which was diminished in PRIP-1-/- mice. PRIP-1-/- mice exhibited enhanced PP1alpha activity compared with controls. Furthermore, PRIP-1 was able to interact directly with GABA(A) receptor beta subunits, and moreover, these proteins were found to be PP1alpha substrates. Finally, phosphorylation of PRIP-1 on threonine 94 facilitated the dissociation of PP1alpha-PRIP-1 complexes, providing a local mechanism for the activation of PP1alpha. Together, these results suggest an essential role for PRIP-1 in controlling GABA(A) receptor activity via regulating subunit phosphorylation and thereby the efficacy of neuronal inhibition mediated by these receptors.

Indexed as

AnimalsCalcium ChannelsCyclic AMP-Dependent Protein KinasesHippocampusInositol 1,4,5-Trisphosphate ReceptorsIn Vitro TechniquesMiceMice, KnockoutPatch-Clamp TechniquesPhosphoprotein PhosphatasesPhosphorylationProtein Phosphatase 1Protein SubunitsReceptors, Cytoplasmic and NuclearReceptors, Dopamine D1Receptors, GABA-ACalcium ChannelsCyclic AMP-Dependent Protein KinasesInositol 1,4,5-Trisphosphate ReceptorsPhosphoprotein PhosphatasesProtein Phosphatase 1Protein SubunitsReceptors, Cytoplasmic and NuclearReceptors, Dopamine D1Receptors, GABA-A

Identifiers

PMID15306641
PMCPMC6729171
OpenAlexW2103208153

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.