Evidence map›Paper›PMID 19209902›Full record

ArticleJournal of proteome research2009

Identification of phosphorylation-dependent binding partners of aquaporin-2 using protein mass spectrometry.

Nicholas A Zwang, Jason D Hoffert, Trairak Pisitkun, Hanne B Moeller, Robert A Fenton, Mark A Knepper

Open access · greenAbstract read
In one paragraph

Article in Journal of proteome research, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

20 citing papers in PubMed, 50 citations in OpenAlex.

  1. Proteomics and AQP2 regulation.The Journal of physiology · 2024
    Review
  2. Insight into the Mammalian Aquaporin Interactome.International journal of molecular sciences · 2022
    Review
  3. Review
  4. Review
  5. Article
  6. Review
  7. Article
  8. Aquaporin Protein-Protein Interactions.International journal of molecular sciences · 2017
    Review
  9. Article
  10. Article
  11. Article
  12. Molecular mechanisms regulating aquaporin-2 in kidney collecting duct.American journal of physiology. Renal physiology · 2016
    Review
  13. Review
  14. Review
  15. Article
  16. Cell biology of vasopressin-regulated aquaporin-2 trafficking.Pflugers Archiv : European journal of physiology · 2012
    Review
  17. Review
  18. Article
  19. Phosphorylation of aquaporin-2 regulates its endocytosis and protein-protein interactions.Proceedings of the National Academy of Sciences of the United States of America · 2010
    Article
  20. Aquaporin-2 in the "-omics" era.The Journal of biological chemistry · 2009
    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.

Nicholas A ZwangLaboratory of Kidney and Electrolyte Metabolism, National Heart, Lung and Blood Institute, National Institutes of Health, Bethesda, Maryland 20892, USA.
Jason D Hoffert
Trairak Pisitkun
Hanne B Moeller
Robert A Fenton
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
Proteomics CoreZICHL005903 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI GUCEK, MARJAN · 2009 to 2022
$23.3M
SOLUTE AND WATER TRANSPORT IN RENAL EPITHELIAZ01HL001285 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI KNEPPER, MARK A · 1998 to 2008
$3.8M
Howard Hughes Medical InstituteIntramural NIH HHS Z01 HL001285Intramural NIH HHS Z99 HL999999NHLBI NIH HHS Z01-HL-01285-KE
6 · The paper itself

Abstract

Vasopressin-mediated control of water permeability in the renal collecting duct occurs in part through regulation of the distribution of aquaporin-2 (AQP2) between the apical plasma membrane and intracellular membrane compartments. Phosphorylation of Ser-256 at AQP2's cytoplasmic COOH-terminus is well-accepted as a critical step for translocation. The aim of this study was to identify binding partners to phosphorylated versus nonphosphorylated forms of the AQP2 COOH-terminus via a targeted comparative proteomic approach. Cytosol from inner medullary collecting ducts isolated from rat kidneys was incubated with "bait" peptides, representing the COOH-terminal AQP2 tail in its nonphosphorylated and phosphorylated forms, to capture differentially bound proteins prior to LC-MS/MS analysis. Mass spectrometric results were confirmed by immunoblotting. Immunoprecipitation was performed using an AQP2 COOH-terminal antibody combined with immunblotting against the proposed binding partners to demonstrate interactions with native AQP2. Our studies confirmed previously identified interactions between AQP2 and hsc70, hsp70-1 and -2, as well as annexin II. These proteins were found to bind less to the Ser-256-phosphorylated AQP2 than to the nonphosphorylated form. In contrast, another heat shock protein, hsp70-5 (BiP/grp78), bound to phosphorylated AQP2 more avidly than to nonphosphorylated AQP2. Immunogold EM studies demonstrated that BiP is present not only in the ER but also in the cytoplasm and apical plasma membrane of rat collecting duct cells. Furthermore, confocal immunofluorescence studies showed partial colocalization of BiP with AQP2 in non-ER compartments. These results suggest that phosphorylation of AQP2 at Ser-256 may regulate AQP2 trafficking in part by mediating differential binding of hsp70 family proteins to the COOH-terminal tail.

Indexed as

Amino Acid SequenceAnimalsAquaporin 2Chromatography, LiquidKidneyMaleMolecular Sequence DataPhosphorylationProtein BindingProtein TransportRatsRats, Sprague-DawleyTandem Mass SpectrometryAqp2 protein, ratAquaporin 2

Identifiers

PMID19209902
PMCPMC2693456
OpenAlexW2048824434

What OpenQuestion holds

Textmetadata
LicenceTDM
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.