Evidence map›Paper›PMID 22992673›Full record

ArticleAmerican journal of physiology. Cell physiology2012

Quantitative phosphoproteomics in nuclei of vasopressin-sensitive renal collecting duct cells.

Steven J Bolger, Patricia A Gonzales Hurtado, Jason D Hoffert, Fahad Saeed, Trairak Pisitkun, Mark A Knepper

Abstract read
In one paragraph

Article in American journal of physiology. Cell physiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

19 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
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  3. Review
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  5. Article
  6. Review
  7. Article
  8. Genome-Wide Mapping of DNA Accessibility and Binding Sites for CREB and C/EBPJournal of the American Society of Nephrology : JASN · 2018
    Article
  9. Article
  10. Article
  11. Article
  12. Article
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  15. Article
  16. Review
  17. Article
  18. Article
  19. Vasopressin and the regulation of aquaporin-2.Clinical and experimental nephrology · 2013
    Review
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.

Steven J BolgerEpithelial Systems Biology Laboratory, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892-1603, USA.
Patricia A Gonzales Hurtado
Jason D Hoffert
Fahad Saeed
Trairak Pisitkun
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 HHSNHLBI NIH HHS Z01-HL001285
6 · The paper itself

Abstract

Vasopressin regulates transport across the collecting duct epithelium in part via effects on gene transcription. Transcriptional regulation occurs partially via changes in phosphorylation of transcription factors, transcriptional coactivators, and protein kinases in the nucleus. To test whether vasopressin alters the nuclear phosphoproteome of vasopressin-sensitive cultured mouse mpkCCD cells, we used stable isotope labeling and mass spectrometry to quantify thousands of phosphorylation sites in nuclear extracts and nuclear pellet fractions. Measurements were made in the presence and absence of the vasopressin analog dDAVP. Of the 1,251 sites quantified, 39 changed significantly in response to dDAVP. Network analysis of the regulated proteins revealed two major clusters ("cell-cell adhesion" and "transcriptional regulation") that were connected to known elements of the vasopressin signaling pathway. The hub proteins for these two clusters were the transcriptional coactivator β-catenin and the transcription factor c-Jun. Phosphorylation of β-catenin at Ser552 was increased by dDAVP [log(2)(dDAVP/vehicle) = 1.79], and phosphorylation of c-Jun at Ser73 was decreased [log(2)(dDAVP/vehicle) = -0.53]. The β-catenin site is known to be targeted by either protein kinase A or Akt, both of which are activated in response to vasopressin. The c-Jun site is a canonical target for the MAP kinase Jnk2, which is downregulated in response to vasopressin in the collecting duct. The data support the idea that vasopressin-mediated control of transcription in collecting duct cells involves selective changes in the nuclear phosphoproteome. All data are available to users at http://helixweb.nih.gov/ESBL/Database/mNPPD/.

Indexed as

Amino Acid SequenceAnimalsCell LineCell NucleusComputational BiologyKidney Tubules, CollectingMicePhosphopeptidesProteomicsTranscriptomeVasopressinsPhosphopeptidesVasopressins

Identifiers

PMID22992673
PMCPMC3492837
OpenAlexW2069730161

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.