Evidence map›Paper›PMID 20716524›Full record

ArticleThe Journal of biological chemistry2010

Regulation of the AGS3·G{alpha}i signaling complex by a seven-transmembrane span receptor.

Sukru Sadik Oner, Ningfei An, Ali Vural, Billy Breton, Michel Bouvier, Joe B Blumer, Stephen M Lanier

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
2.4field-weighted citation impact, top 12% 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

36 citing papers in PubMed, 50 citations in OpenAlex.

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  14. Regulation of Chemokine Signal Integration by Activator of G-Protein Signaling 4 (AGS4).The Journal of pharmacology and experimental therapeutics · 2017
    Article
  15. Article
  16. Article
  17. Article
  18. Activators of G protein signaling in the kidney.The Journal of pharmacology and experimental therapeutics · 2015
    Review
  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

7 authors at 2 institutions in 2 countries.

Sukru Sadik OnerDepartment of Cell and Molecular Pharmacology & Experimental Therapeutics, Medical University of South Carolina, Charleston, South Carolina 29425, USA.
Ningfei An
Ali Vural
Billy Breton
Michel Bouvier
Joe B Blumer
Stephen M Lanier
Medical University of South Carolina · USInstitute for Research in Immunology and Cancer · CA

Funding

STRUCTURAL ANALYSIS OF THE ALPHA-2 ADRENERGIC RECEPTORR01NS024821 · NINDS · MEDICAL UNIVERSITY OF SOUTH CAROLINA · PI LANIER, STEPHEN M. · 1994 to 2007
$2.4M
ACCESSORY PROTEINS AND G-PROTEIN SIGNALING MECHANISMSR01DA025896 · NIDA · MEDICAL UNIVERSITY OF SOUTH CAROLINA · PI LANIER, STEPHEN M. · 2008 to 2012
$1.6M
AGS4 in G-protein Signal ProcessingR01GM086510 · NIGMS · MEDICAL UNIVERSITY OF SOUTH CAROLINA · PI BLUMER, JOE B · 2009 to 2013
$1.5M
STRUCTURAL ANALYSIS OF THE ALPHA2-ADRENERGIC RECEPTORR29NS024821 · NINDS · MEDICAL UNIVERSITY OF SOUTH CAROLINA · PI LANIER, STEPHEN M. · 1987 to 1991
–
CIHRNIDA NIH HHS DA025896NIDA NIH HHS R01 DA025896NIGMS NIH HHS GM086510NIGMS NIH HHS R01 GM086510NINDS NIH HHS NS24821NINDS NIH HHS R01 NS024821
6 · The paper itself

Abstract

G-protein signaling modulators (GPSM) play diverse functional roles through their interaction with G-protein subunits. AGS3 (GPSM1) contains four G-protein regulatory motifs (GPR) that directly bind Gα(i) free of Gβγ providing an unusual scaffold for the "G-switch" and signaling complexes, but the mechanism by which signals track into this scaffold are not well understood. We report the regulation of the AGS3·Gα(i) signaling module by a cell surface, seven-transmembrane receptor. AGS3 and Gα(i1) tagged with Renilla luciferase or yellow fluorescent protein expressed in mammalian cells exhibited saturable, specific bioluminescence resonance energy transfer indicating complex formation in the cell. Activation of α(2)-adrenergic receptors or μ-opioid receptors reduced AGS3-RLuc·Gα(i1)-YFP energy transfer by over 30%. The agonist-mediated effects were inhibited by pertussis toxin and co-expression of RGS4, but were not altered by Gβγ sequestration with the carboxyl terminus of GRK2. Gα(i)-dependent and agonist-sensitive bioluminescence resonance energy transfer was also observed between AGS3 and cell-surface receptors typically coupled to Gα(i) and/or Gα(o) indicating that AGS3 is part of a larger signaling complex. Upon receptor activation, AGS3 reversibly dissociates from this complex at the cell cortex. Receptor coupling to both Gαβγ and GPR-Gα(i) offer additional flexibility for systems to respond and adapt to challenges and orchestrate complex behaviors.

Indexed as

Signal TransductionAnimalsCarrier ProteinsCell LineCell MembraneGene Expression RegulationGTP-Binding Protein alpha Subunits, Gi-GoGuanine Nucleotide Dissociation InhibitorsHumansMembrane ProteinsModels, BiologicalProtein BindingProtein Structure, TertiaryReceptors, Adrenergic, alpha-2Receptors, Opioid, muRenillaCarrier ProteinsGPSM1 protein, humanGTP-Binding Protein alpha Subunits, Gi-GoGuanine Nucleotide Dissociation InhibitorsMembrane ProteinsReceptors, Adrenergic, alpha-2Receptors, Opioid, mu

Identifiers

PMID20716524
PMCPMC2962495
OpenAlexW1496900694

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.