Evidence map›Paper›PMID 20724536›Full record

ArticleJournal of the American Society of Nephrology : JASN2010

Reciprocal regulation of aquaporin-2 abundance and degradation by protein kinase A and p38-MAP kinase.

Pavel I Nedvetsky, Vedrana Tabor, Grazia Tamma, Sven Beulshausen, Philipp Skroblin, Aline Kirschner, Kerim Mutig, Mareike Boltzen, Oscar Petrucci, Anna Vossenkämper and 4 more

Open access · greenAbstract read
In one paragraph

Article in Journal of the American Society of Nephrology : JASN, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 papers.

0numbers the graph read from it
0cells of the map it votes in
72citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

72 citing papers in PubMed, 111 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Proteomics and AQP2 regulation.The Journal of physiology · 2024
    Review
  8. Article
  9. Regulation of the water channel aquaporin-2 by cullin E3 ubiquitin ligases.American journal of physiology. Renal physiology · 2024
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Clinical, Genetic and Functional Characterization of a NovelJournal of personalized medicine · 2022
    Article
  16. Article
  17. Review
  18. Article
  19. Review
  20. Rapid development of vasopressin resistance in dietary KAmerican journal of physiology. Renal physiology · 2021
    Article

12 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

14 authors at 4 institutions in 2 countries.

Pavel I NedvetskyLeibniz-Institute for Molecular Pharmacology, Berlin, Germany. Pavel.Nedvetsky@ucsf.edu
Vedrana Tabor
Grazia Tamma
Sven Beulshausen
Philipp Skroblin
Aline Kirschner
Kerim Mutig
Mareike Boltzen
Oscar Petrucci
Anna Vossenkämper
Burkhard Wiesner
Sebastian Bachmann
Walter Rosenthal
Enno Klussmann
Leibniz Association · DEHumboldt-Universität zu Berlin · DECharité - Universitätsmedizin Berlin · DEUniversity of Bari Aldo Moro · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Arginine-vasopressin (AVP) modulates the water channel aquaporin-2 (AQP2) in the renal collecting duct to maintain homeostasis of body water. AVP binds to vasopressin V2 receptors (V2R), increasing cAMP, which promotes the redistribution of AQP2 from intracellular vesicles into the plasma membrane. cAMP also increases AQP2 transcription, but whether altered degradation also modulates AQP2 protein levels is not well understood. Here, elevation of cAMP increased AQP2 protein levels within 30 minutes in primary inner medullary collecting duct (IMCD) cells, in human embryonic kidney (HEK) 293 cells ectopically expressing AQP2, and in mouse kidneys. Accelerated transcription or translation did not explain this increase in AQP2 abundance. In IMCD cells, cAMP inhibited p38-mitogen-activated protein kinase (p38-MAPK) via activation of protein kinase A (PKA). Inhibition of p38-MAPK associated with decreased phosphorylation (serine 261) and polyubiquitination of AQP2, preventing proteasomal degradation. Our results demonstrate that AVP enhances AQP2 protein abundance by altering its proteasomal degradation through a PKA- and p38-MAPK-dependent pathway.

Indexed as

AnimalsAquaporin 2Arginine VasopressinCell LineColforsinCyclic AMPCyclic AMP-Dependent Protein KinasesHumansKidney MedullaKidney Tubules, CollectingMiceMice, Inbred C57BLp38 Mitogen-Activated Protein KinasesPhosphorylationProteasome Endopeptidase ComplexProtein BiosynthesisAquaporin 2Arginine VasopressinColforsinCyclic AMPCyclic AMP-Dependent Protein Kinasesp38 Mitogen-Activated Protein KinasesProteasome Endopeptidase Complex

Identifiers

PMID20724536
PMCPMC3013543
OpenAlexW2104124436

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.