Evidence map›Paper›PMID 26786101›Full record

ArticleThe Journal of biological chemistry2016

Structural Determinants of Oligomerization of the Aquaporin-4 Channel.

Philip Kitchen, Matthew T Conner, Roslyn M Bill, Alex C Conner

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

28 citing papers in PubMed, 36 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Aquaporins in the Capillaries of the Dura Mater of Pigs.International journal of molecular sciences · 2025
    Article
  6. Article
  7. Article
  8. Article
  9. Anomalous Oligomerization Behavior ofInternational journal of molecular sciences · 2023
    Article
  10. Aquaporin-5 Dynamic Regulation.International journal of molecular sciences · 2023
    Review
  11. Review
  12. Insight into the Mammalian Aquaporin Interactome.International journal of molecular sciences · 2022
    Review
  13. Molecular mechanisms governing aquaporin relocalisation.Biochimica et biophysica acta. Biomembranes · 2022
    Review
  14. Article
  15. Review
  16. Review
  17. Article
  18. Review
  19. Article
  20. 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

4 authors at 3 institutions in 1 country.

Philip KitchenFrom the Molecular Assembly and Organisation in Cells Doctoral Training Centre, University of Warwick, Coventry CV4 7AL, the School of Life & Health Sciences and Aston Research Centre for Healthy Ageing, Aston University, Aston Triangle, Birmingham, B4 7ET, and the Institute of Clinical Sciences, University of Birmingham, Edgbaston, Birmingham B15 2TT, United Kingdom.
Matthew T Connerthe School of Biology, Chemistry and Forensic Science, Faculty of Science and Engineering, University of Wolverhampton, Wolverhampton WV1 1LY.
Roslyn M Billthe School of Life & Health Sciences and Aston Research Centre for Healthy Ageing, Aston University, Aston Triangle, Birmingham, B4 7ET, and r.m.bill@aston.ac.uk.
Alex C Connerthe Institute of Clinical Sciences, University of Birmingham, Edgbaston, Birmingham B15 2TT, United Kingdom a.c.conner@bham.ac.uk.
University of Birmingham · GBAston University · GBUniversity of Wolverhampton · GB

Funding

Biotechnology and Biological Sciences Research Council BB/I019960/1Biotechnology and Biological Sciences Research Council BB/K013319/1Biotechnology and Biological Sciences Research Council BB/L502194/1
6 · The paper itself

Abstract

The aquaporin (AQP) family of integral membrane protein channels mediate cellular water and solute flow. Although qualitative and quantitative differences in channel permeability, selectivity, subcellular localization, and trafficking responses have been observed for different members of the AQP family, the signature homotetrameric quaternary structure is conserved. Using a variety of biophysical techniques, we show that mutations to an intracellular loop (loop D) of human AQP4 reduce oligomerization. Non-tetrameric AQP4 mutants are unable to relocalize to the plasma membrane in response to changes in extracellular tonicity, despite equivalent constitutive surface expression levels and water permeability to wild-type AQP4. A network of AQP4 loop D hydrogen bonding interactions, identified using molecular dynamics simulations and based on a comparative mutagenic analysis of AQPs 1, 3, and 4, suggest that loop D interactions may provide a general structural framework for tetrameric assembly within the AQP family.

Indexed as

Amino Acid SequenceAnimalsAquaporin 1Aquaporin 3Aquaporin 4Cloning, MolecularCrystallography, X-RayDogsEscherichia coliGene ExpressionHEK293 CellsHumansHydrogen BondingMadin Darby Canine Kidney CellsMolecular Dynamics SimulationMolecular Sequence DataAQP1 protein, humanAQP3 protein, humanAQP4 protein, humanAquaporin 1Aquaporin 3Aquaporin 4Recombinant ProteinsWateraquaporincellular regulationoligomerizationprotein translocationwater channel

Identifiers

PMID26786101
PMCPMC4807272
OpenAlexW2283938713

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.