Evidence map›Paper›PMID 26013827›Full record

ArticleThe Journal of biological chemistry2015

Identification and Molecular Mechanisms of the Rapid Tonicity-induced Relocalization of the Aquaporin 4 Channel.

Philip Kitchen, Rebecca E Day, Luke H J Taylor, Mootaz M Salman, Roslyn M Bill, Matthew T Conner, Alex C Conner

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. 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
3.2field-weighted citation impact, top 8% 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, 105 citations in OpenAlex.

  1. Article
  2. LRBA organizes distinct vesicular trafficking systems in distal nephron segments for water and sodium conservation.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  3. Adenosine AJournal of neurochemistry · 2026
    Article
  4. Article
  5. Article
  6. Review
  7. Aquaporin-4 in Stroke and Brain Edema-Friend or Foe?International journal of molecular sciences · 2025
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
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  18. Article
  19. Article
  20. Review

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

7 authors at 4 institutions in 1 country.

Philip KitchenFrom the Molecular Organisation and Assembly in Cells Doctoral Training Centre, University of Warwick, Coventry CV4 7AL.
Rebecca E Daythe Biomedical Research Centre, Sheffield Hallam University, Howard Street, Sheffield S1 1WB.
Luke H J TaylorFrom the Molecular Organisation and Assembly in Cells Doctoral Training Centre, University of Warwick, Coventry CV4 7AL.
Mootaz M Salmanthe Biomedical Research Centre, Sheffield Hallam University, Howard Street, Sheffield S1 1WB.
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.
Matthew T Connerthe Biomedical Research Centre, Sheffield Hallam University, Howard Street, Sheffield S1 1WB, m.conner@shu.ac.uk.
Alex C Connerthe School of Clinical and Experimental Medicine, University of Birmingham, Edgbaston, Birmingham B15 2TT, United Kingdom a.c.conner@bham.ac.uk.
Sheffield Hallam University · GBUniversity of Warwick · GBAston University · GBUniversity of Birmingham · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The aquaporin family of integral membrane proteins is composed of channels that mediate cellular water flow. Aquaporin 4 (AQP4) is highly expressed in the glial cells of the central nervous system and facilitates the osmotically driven pathological brain swelling associated with stroke and traumatic brain injury. Here we show that AQP4 cell surface expression can be rapidly and reversibly regulated in response to changes of tonicity in primary cortical rat astrocytes and in transfected HEK293 cells. The translocation mechanism involves PKA activation, influx of extracellular calcium, and activation of calmodulin. We identify five putative PKA phosphorylation sites and use site-directed mutagenesis to show that only phosphorylation at one of these sites, serine 276, is necessary for the translocation response. We discuss our findings in the context of the identification of new therapeutic approaches to treating brain edema.

Indexed as

Amino Acid MotifsAnimalsAquaporin 4AstrocytesBrain EdemaCalciumCalmodulinCells, CulturedCyclic AMP-Dependent Protein KinasesHEK293 CellsHumansOsmotic PressurePhosphorylationProtein TransportRatsAquaporin 4CalciumCalmodulinCyclic AMP-Dependent Protein Kinasesaquaporinastrocytehomeostasishypotonicityprotein translocationrapid traffickingregulationwater channel

Identifiers

PMID26013827
PMCPMC4505433
OpenAlexW1818228426

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.