Evidence map›Paper›PMID 23770668›Full record

ArticleThe Journal of biological chemistry2013

Translocation of activator of G-protein signaling 3 to the Golgi apparatus in response to receptor activation and its effect on the trans-Golgi network.

Sukru S Oner, Ali Vural, Stephen M Lanier

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing 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

17 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Activators of G protein signaling in the kidney.The Journal of pharmacology and experimental therapeutics · 2015
    Review
  13. Article
  14. Gαi3-Dependent Inhibition of JNK Activity on Intracellular Membranes.Frontiers in bioengineering and biotechnology · 2015
    Article
  15. Article
  16. Review
  17. 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

3 authors.

Sukru S OnerDepartment of Cell and Molecular Pharmacology and Experimental Therapeutics, Medical University of South Carolina, Charleston, South Carolina 29425, USA.
Ali Vural
Stephen M Lanier

Funding

ACCESSORY PROTEINS AND G-PROTEIN SIGNALING MECHANISMSR01DA025896 · NIDA · MEDICAL UNIVERSITY OF SOUTH CAROLINA · PI LANIER, STEPHEN M. · 2008 to 2012
$1.6M
NIDA NIH HHS DA025896NIDA NIH HHS R01 DA025896
6 · The paper itself

Abstract

Group II activators of G-protein signaling play diverse functional roles through their interaction with Gαi, Gαt, and Gαo via a G-protein regulatory (GPR) motif that serves as a docking site for Gα-GDP. We recently reported the regulation of the AGS3-Gαi signaling module by a cell surface, seven-transmembrane receptor. Upon receptor activation, AGS3 reversibly dissociates from the cell cortex, suggesting that it may function as a signal transducer with downstream signaling implications, and this question is addressed in the current report. In HEK-293 and COS-7 cells expressing the α2A/D-AR and Gαi3, receptor activation resulted in the translocation of endogenous AGS3 and AGS3-GFP from the cell cortex to a juxtanuclear region, where it co-localized with markers of the Golgi apparatus (GA). The agonist-induced translocation of AGS3 was reversed by the α2-AR antagonist rauwolscine. The TPR domain of AGS3 was required for agonist-induced translocation of AGS3 from the cell cortex to the GA, and the translocation was blocked by pertussis toxin pretreatment or by the phospholipase Cβ inhibitor U73122. Agonist-induced translocation of AGS3 to the GA altered the functional organization and protein sorting at the trans-Golgi network. The regulated movement of AGS3 between the cell cortex and the GA offers unexpected mechanisms for modulating protein secretion and/or endosome recycling events at the trans-Golgi network.

Indexed as

AnimalsBiomarkersBrimonidine TartrateCell MembraneChlorocebus aethiopsCOS CellsEndosomesGreen Fluorescent ProteinsGTP-Binding Protein alpha Subunits, Gi-GoGuanine Nucleotide Dissociation InhibitorsHEK293 CellsHumansLysosomesProtein Structure, TertiaryProtein TransportQuinoxalinesBiomarkersBrimonidine TartrateGPSM1 protein, humanGreen Fluorescent ProteinsGTP-Binding Protein alpha Subunits, Gi-GoGuanine Nucleotide Dissociation InhibitorsQuinoxalinesReceptors, Cell SurfaceActivator of G-protein Signaling 3AGS3-Gαi ComplexGolgiGPR MotifG-protein-coupled Receptors (GPCR)G-proteinsSecretory PathwaySignal TransductionTraffickingtrans-Golgi Network

Identifiers

PMID23770668
PMCPMC3745352

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.