Evidence map›Paper›PMID 30404823›Full record

ArticleJournal of cell science2018

Role of G-proteins and phosphorylation in the distribution of AGS3 to cell puncta.

Ali Vural, Ersin Fadillioglu, Fatih Kelesoglu, Dzwokai Ma, Stephen M Lanier

Open access · bronzeAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of cell science, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.7field-weighted citation impact, top 29% 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

7 citing papers in PubMed, 12 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. AGS3 and GαMolecules (Basel, Switzerland) · 2020
    Article
  7. 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

5 authors at 3 institutions in 1 country.

Ali VuralDepartment of Pharmacology, Wayne State University School of Medicine, Detroit, MI 48201, USA ali.vural@wayne.edu lanier@wayne.edu.
Ersin FadilliogluDepartment of Cell and Molecular Pharmacology and Experimental Therapeutics, Medical University of South Carolina, Charleston, SC 29425, USA.ORCID 0000-0001-7867-8477
Fatih KelesogluDepartment of Cell and Molecular Pharmacology and Experimental Therapeutics, Medical University of South Carolina, Charleston, SC 29425, USA.
Dzwokai MaDepartment of Molecular, Cellular, and Developmental Biology, Neuroscience Research Institute, University of California, Santa Barbara, Santa Barbara, CA 93106, USA.
Stephen M LanierDepartment of Pharmacology, Wayne State University School of Medicine, Detroit, MI 48201, USA ali.vural@wayne.edu lanier@wayne.edu.ORCID 0000-0002-2740-7607
Medical University of South Carolina · USUniversity of California, Santa Barbara · USWayne State University · US

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
mDpy-30, intracellular protein transport, and histone methylationR21MH086853 · NIMH · UNIVERSITY OF CALIFORNIA SANTA BARBARA · PI MA, DZWOKAI Z · 2010 to 2011
$388k
NIDA NIH HHS R01 DA025896NIMH NIH HHS R21 MH086853NINDS NIH HHS R01 NS024821
6 · The paper itself

Abstract

Activator of G-protein signaling 3 (AGS3, also known as GPSM1) exhibits broad functional diversity and oscillates among different subcellular compartments in a regulated manner. AGS3 consists of a tetratricopeptide repeat (TPR) domain and a G-protein regulatory (GPR) domain. Here, we tested the hypothesis that phosphorylation of the AGS3 GPR domain regulates its subcellular distribution and functionality. In contrast to the cortical and/or diffuse non-homogeneous distribution of wild-type (WT) AGS3, an AGS3 construct lacking all 24 potential phosphorylation sites in the GPR domain localized to cytosolic puncta. This change in localization was revealed to be dependent upon phosphorylation of a single threonine amino acid (T602). The punctate distribution of AGS3-T602A was rescued by co-expression of Gα

Indexed as

AnimalsGTP-Binding ProteinsGuanine Nucleotide Dissociation InhibitorsPhosphorylationSignal TransductionGPSM1 protein, humanGTP-Binding ProteinsGuanine Nucleotide Dissociation InhibitorsActivators of G-protein signaling 3AggresomeCytosolic punctaG-protein regulatory domainPhase transitionPhosphorylation

Identifiers

PMID30404823
PMCPMC6288075
OpenAlexW2900377421

What Socratic 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 Socratic graph.