Evidence map›Paper›PMID 27760771›Full record

ReviewAmerican journal of physiology. Renal physiology2016

Molecular mechanisms regulating aquaporin-2 in kidney collecting duct.

Hyun Jun Jung, Tae-Hwan Kwon

Open access · bronzeAbstract readReview
In one paragraph

Review in American journal of physiology. Renal physiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.

0numbers the graph read from it
0cells of the map it votes in
62citing papers in PubMed
6.3field-weighted citation impact, top 3% 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

62 citing papers in PubMed, 112 citations in OpenAlex.

  1. Transcriptional regulatory factors of the Aqp2 gene.Kidney research and clinical practice · 2026
    Article
  2. Article
  3. Vasopressin-Sensitive Aqp2 Regulation Mediated by the TAZ-NR4A1 Axis in Renal Collecting Duct Cells.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025
    Article
  4. Article
  5. Article
  6. Proteomics and AQP2 regulation.The Journal of physiology · 2024
    Review
  7. Article
  8. Intercalated cell function, kidney innate immunity, and urinary tract infections.Pflugers Archiv : European journal of physiology · 2024
    Review
  9. Article
  10. Article
  11. Article
  12. Genome-Engineered mpkCCDc14 Cells as a New Resource for Studying AQP2.International journal of molecular sciences · 2023
    Article
  13. Article
  14. Article
  15. Differentiated mouse kidney tubuloids as a novelFrontiers in cell and developmental biology · 2023
    Article
  16. Article
  17. Organs-on-chip technology: a tool to tackle genetic kidney diseases.Pediatric nephrology (Berlin, Germany) · 2022
    Review
  18. Pathophysiology of Drug-Induced Hyponatremia.Journal of clinical medicine · 2022
    Review
  19. Article
  20. Review

2 more citing papers are in PubMed but not listed here.

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

2 authors at 2 institutions in 2 countries.

Hyun Jun JungEpithelial Systems Biology Laboratory, Systems Biology Center, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, Maryland; and.
Tae-Hwan KwonDepartment of Biochemistry and Cell Biology, School of Medicine, Kyungpook National University, Taegu, Korea thkwon@knu.ac.kr.
Kyungpook National University · KRNational Institutes of Health · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The kidney collecting duct is an important renal tubular segment for regulation of body water homeostasis and urine concentration. Water reabsorption in the collecting duct principal cells is controlled by vasopressin, a peptide hormone that induces the osmotic water transport across the collecting duct epithelia through regulation of water channel proteins aquaporin-2 (AQP2) and aquaporin-3 (AQP3). In particular, vasopressin induces both intracellular translocation of AQP2-bearing vesicles to the apical plasma membrane and transcription of the Aqp2 gene to increase AQP2 protein abundance. The signaling pathways, including AQP2 phosphorylation, RhoA phosphorylation, intracellular calcium mobilization, and actin depolymerization, play a key role in the translocation of AQP2. This review summarizes recent data demonstrating the regulation of AQP2 as the underlying molecular mechanism for the homeostasis of water balance in the body.

Indexed as

AnimalsAquaporin 2Aquaporin 3Body WaterHomeostasisHumansKidney Tubules, CollectingPhosphorylationSignal TransductionWater-Electrolyte BalanceAquaporin 2Aquaporin 3aquaporin-2arginine vasopressinbody water balanceintracellular trafficking

Identifiers

PMID27760771
PMCPMC5243240
OpenAlexW2535297938

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.