Evidence map›Paper›PMID 28710278›Full record

ArticleThe Journal of biological chemistry2017

Phosphorylation of human aquaporin 2 (AQP2) allosterically controls its interaction with the lysosomal trafficking protein LIP5.

Jennifer Virginia Roche, Sabeen Survery, Stefan Kreida, Veronika Nesverova, Henry Ampah-Korsah, Maria Gourdon, Peter M T Deen, Susanna Törnroth-Horsefield

Open access · hybridAbstract readComparative Study
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 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

24 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Aquaporins: a novel perspective in the treatment of lung diseases.Inflammation research : official journal of the European Histamine Research Society ... [et al.] · 2025
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Methods for studying mammalian aquaporin biology.Biology methods & protocols · 2023
    Review
  12. Article
  13. Insight into the Mammalian Aquaporin Interactome.International journal of molecular sciences · 2022
    Review
  14. Article
  15. Molecular mechanisms governing aquaporin relocalisation.Biochimica et biophysica acta. Biomembranes · 2022
    Review
  16. Review
  17. Review
  18. Article
  19. Article
  20. Structural Insights into AQP2 Targeting to Multivesicular Bodies.International journal of molecular sciences · 2019
    Article
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

8 authors at 2 institutions in 3 countries.

Jennifer Virginia RocheFrom the Department of Biochemistry and Structural Biology, Lund University, 221 00 Lund, Sweden and.
Sabeen SurveryFrom the Department of Biochemistry and Structural Biology, Lund University, 221 00 Lund, Sweden and.
Stefan KreidaFrom the Department of Biochemistry and Structural Biology, Lund University, 221 00 Lund, Sweden and.
Veronika NesverovaFrom the Department of Biochemistry and Structural Biology, Lund University, 221 00 Lund, Sweden and.
Henry Ampah-KorsahFrom the Department of Biochemistry and Structural Biology, Lund University, 221 00 Lund, Sweden and.
Maria GourdonFrom the Department of Biochemistry and Structural Biology, Lund University, 221 00 Lund, Sweden and.
Peter M T Deenthe Department of Physiology, Radboud University Medical Center, 6525 GA Nijmegen, The Netherlands.
Susanna Törnroth-HorsefieldFrom the Department of Biochemistry and Structural Biology, Lund University, 221 00 Lund, Sweden and susanna.horsefield@biochemistry.lu.se.ORCID 0000-0002-9435-8243
Lund University · SERadboud University Nijmegen · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The interaction between the renal water channel aquaporin-2 (AQP2) and the lysosomal trafficking regulator-interacting protein LIP5 targets AQP2 to multivesicular bodies and facilitates lysosomal degradation. This interaction is part of a process that controls AQP2 apical membrane abundance in a vasopressin-dependent manner, allowing for urine volume adjustment. Vasopressin regulates phosphorylation at four sites within the AQP2 C terminus (Ser

Indexed as

Models, MolecularProtein Processing, Post-TranslationalAllosteric RegulationAmino Acid SubstitutionAquaporin 2Binding SitesEndosomal Sorting Complexes Required for TransportGene DeletionHumansMutationPeptide FragmentsPhosphorylationPichiaProtein ConformationProtein Interaction Domains and MotifsProtein MultimerizationAQP2 protein, humanAquaporin 2Endosomal Sorting Complexes Required for TransportPeptide FragmentsRecombinant Fusion ProteinsVTA1 protein, humanaquaporinmembrane proteinmembrane traffickingphosphorylationprotein-protein interaction

Identifiers

PMID28710278
PMCPMC5582854
OpenAlexW2734724933

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.