Evidence map›Paper›PMID 28336531›Full record

ArticleThe Journal of biological chemistry2017

Vasopressin-induced serine 269 phosphorylation reduces Sipa1l1 (signal-induced proliferation-associated 1 like 1)-mediated aquaporin-2 endocytosis.

Po-Jen Wang, Shu-Ting Lin, Shao-Hsuan Liu, Kuang-Ting Kuo, Chun-Hua Hsu, Mark A Knepper, Ming-Jiun Yu

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.1field-weighted citation impact, top 23% 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

17 citing papers in PubMed, 29 citations in OpenAlex.

  1. GPR39 activation inhibits AQP2 trafficking and alters cytoskeletal organization.American journal of physiology. Cell physiology · 2026
    Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Insight into the Mammalian Aquaporin Interactome.International journal of molecular sciences · 2022
    Review
  8. A multiscale model of the regulation of aquaporin 2 recycling.NPJ systems biology and applications · 2022
    Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. 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

7 authors at 2 institutions in 2 countries.

Po-Jen WangFrom the Institute of Biochemistry and Molecular Biology, National Taiwan University College of Medicine, Taipei 10051, Taiwan.
Shu-Ting LinFrom the Institute of Biochemistry and Molecular Biology, National Taiwan University College of Medicine, Taipei 10051, Taiwan.
Shao-Hsuan LiuFrom the Institute of Biochemistry and Molecular Biology, National Taiwan University College of Medicine, Taipei 10051, Taiwan.
Kuang-Ting KuoFrom the Institute of Biochemistry and Molecular Biology, National Taiwan University College of Medicine, Taipei 10051, Taiwan.
Chun-Hua Hsuthe Department of Agricultural Chemistry, National Taiwan University, Taipei 10617, Taiwan, and.
Mark A Knepperthe Systems Biology Center, NHLBI, National Institutes of Health, Bethesda, Maryland 20892-1603.
Ming-Jiun YuFrom the Institute of Biochemistry and Molecular Biology, National Taiwan University College of Medicine, Taipei 10051, Taiwan, mjyu@ntu.edu.tw.
National Taiwan University · TWNational Heart Lung and Blood Institute · 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
Intramural NIH HHS ZIA HL001285Intramural NIH HHS ZIA HL006129
6 · The paper itself

Abstract

The abundance of integral membrane proteins in the plasma membrane is determined by a dynamic balance between exocytosis and endocytosis, which can often be regulated by physiological stimuli. Here, we describe a mechanism that accounts for the ability of the peptide hormone vasopressin to regulate water excretion via a phosphorylation-dependent modulation of the PDZ domain-ligand interaction involving the water channel protein aquaporin-2. We discovered that the PDZ domain-containing protein Sipa1l1 (signal-induced proliferation-associated 1 like 1) binds to the cytoplasmic PDZ-ligand motif of aquaporin-2 and accelerates its endocytosis in the absence of vasopressin. Vasopressin-induced aquaporin-2 phosphorylation within the type I PDZ-ligand motif disrupted the interaction, in association with reduced aquaporin-2 endocytosis and prolonged plasma membrane aquaporin-2 retention. This phosphorylation-dependent alteration in the PDZ domain-ligand interaction was explained by 3D structural models, which showed a hormone-regulated mechanism that controls osmotic water transport and systemic water balance in mammals.

Indexed as

AnimalsAquaporin 2EndocytosisGTPase-Activating ProteinsHEK293 CellsHumansKidneyKidney Tubules, CollectingLigandsMiceModels, MolecularPhosphorylationProtein BindingProtein ConformationProtein DomainsProtein TransportAqp2 protein, mouseAquaporin 2GTPase-Activating ProteinsLigandsRNA, Small InterferingSerineSipa1l1 protein, mouseVasopressinsWaterAQP2aquaporinkidneyPDZ domainphosphorylationrenal physiologySipa1l1vasopressin

Identifiers

PMID28336531
PMCPMC5427275
OpenAlexW2600430291

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.