Evidence map›Paper›PMID 22108457›Full record

ArticleMolecular & cellular proteomics : MCP2012

Dynamics of the G protein-coupled vasopressin V2 receptor signaling network revealed by quantitative phosphoproteomics.

Jason D Hoffert, Trairak Pisitkun, Fahad Saeed, Jae H Song, Chung-Lin Chou, Mark A Knepper

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2012. 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
4.9field-weighted citation impact, top 4% 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, 78 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. The Biology of Vasopressin.Biomedicines · 2021
    Review
  6. Article
  7. Regulation of cardiac O-GlcNAcylation: More than just nutrient availability.Biochimica et biophysica acta. Molecular basis of disease · 2020
    Review
  8. Article
  9. Germline-Derived Gain-of-Function Variants of GsJournal of the American Society of Nephrology : JASN · 2019
    Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  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

6 authors at 2 institutions in 1 country.

Jason D HoffertEpithelial Systems Biology Laboratory, NHLBI, National Institutes of Health, Bethesda, Maryland 20892, USA.
Trairak Pisitkun
Fahad Saeed
Jae H Song
Chung-Lin Chou
Mark A Knepper
National Heart Lung and Blood Institute · USNational Institutes of Health · US

Funding

Solute And Water Transport In Renal EpitheliaZIAHL001285 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI KNEPPER, MARK · 2009 to 2025
$34.9M
Computational Tools for ProteomicsZIAHL006129 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI KNEPPER, MARK · 2011 to 2025
$8.1M
SOLUTE AND WATER TRANSPORT IN RENAL EPITHELIAZ01HL001285 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI KNEPPER, MARK A · 1998 to 2008
$3.8M
Urinary ExosomesZIAHL006128 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI KNEPPER, MARK · 2011 to 2019
$354k
Intramural NIH HHS Z01 HL001285NHLBI NIH HHS ZO1-HL001285
6 · The paper itself

Abstract

G protein-coupled receptors (GPCRs) regulate diverse physiological processes, and many human diseases are due to defects in GPCR signaling. To identify the dynamic response of a signaling network downstream from a prototypical G(s)-coupled GPCR, the vasopressin V2 receptor, we have carried out multireplicate, quantitative phosphoproteomics with iTRAQ labeling at four time points following vasopressin exposure at a physiological concentration in cells isolated from rat kidney. A total of 12,167 phosphopeptides were identified from 2,783 proteins, with 273 changing significantly in abundance with vasopressin. Two-dimensional clustering of phosphopeptide time courses and Gene Ontology terms revealed that ligand binding to the V2 receptor affects more than simply the canonical cyclic adenosine monophosphate-protein kinase A and arrestin pathways under physiological conditions. The regulated proteins included key components of actin cytoskeleton remodeling, cell-cell adhesion, mitogen-activated protein kinase signaling, Wnt/β-catenin signaling, and apoptosis pathways. These data suggest that vasopressin can regulate an array of cellular functions well beyond its classical role in regulating water and solute transport. These results greatly expand the current view of GPCR signaling in a physiological context and shed new light on potential roles for this signaling network in disorders such as polycystic kidney disease. Finally, we provide an online resource of physiologically regulated phosphorylation sites with dynamic quantitative data (http://helixweb.nih.gov/ESBL/Database/TiPD/index.html).

Indexed as

ProteomicsAnimalsChromatography, LiquidCyclic AMPHumansKidney Tubules, CollectingPhosphopeptidesPhosphoproteinsPhosphorylationProteomeRatsReceptors, G-Protein-CoupledReceptors, VasopressinSignal TransductionSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationCyclic AMPPhosphopeptidesPhosphoproteinsProteomeReceptors, G-Protein-CoupledReceptors, Vasopressin

Identifiers

PMID22108457
PMCPMC3277771
OpenAlexW2015039564

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.