Evidence map›Paper›PMID 25609088›Full record

ArticleMolecular biology of the cell2015

Increased water flux induced by an aquaporin-1/carbonic anhydrase II interaction.

Gonzalo Vilas, Devishree Krishnan, Sampath Kumar Loganathan, Darpan Malhotra, Lei Liu, Megan Rachele Beggs, Patrizia Gena, Giuseppe Calamita, Martin Jung, Richard Zimmermann and 3 more

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

12 citing papers in PubMed, 32 citations in OpenAlex.

  1. Trial
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Review
  8. Adaptable interaction between aquaporin-1 and band 3 reveals a potential role of water channel in blood COFASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2017
    Article
  9. Article
  10. Article
  11. Evidence-based complementary and alternative medicine : eCAM · 2016
    Article
  12. 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

13 authors at 3 institutions in 3 countries.

Gonzalo VilasDepartment of Biochemistry, University of Alberta, Edmonton, AB T6G 1C9, Canada.
Devishree KrishnanDepartment of Physiology, University of Alberta, Edmonton, AB T6G 1C9, Canada Membrane Protein Disease Research Group, University of Alberta, Edmonton, AB T6G 1C9, Canada.
Sampath Kumar LoganathanDepartment of Biochemistry, University of Alberta, Edmonton, AB T6G 1C9, Canada Membrane Protein Disease Research Group, University of Alberta, Edmonton, AB T6G 1C9, Canada.
Darpan MalhotraDepartment of Biochemistry, University of Alberta, Edmonton, AB T6G 1C9, Canada Membrane Protein Disease Research Group, University of Alberta, Edmonton, AB T6G 1C9, Canada.
Lei LiuDepartment of Physiology, University of Alberta, Edmonton, AB T6G 1C9, Canada Membrane Protein Disease Research Group, University of Alberta, Edmonton, AB T6G 1C9, Canada.
Megan Rachele BeggsDepartment of Physiology, University of Alberta, Edmonton, AB T6G 1C9, Canada Membrane Protein Disease Research Group, University of Alberta, Edmonton, AB T6G 1C9, Canada.
Patrizia GenaDepartment of Biosciences, Biotechnologies and Biopharmaceutics, University of Bari, 70121 Bari, Italy.
Giuseppe CalamitaDepartment of Biosciences, Biotechnologies and Biopharmaceutics, University of Bari, 70121 Bari, Italy.
Martin JungDepartment of Medical Biochemistry and Molecular Biology, Saarland University, D-66424 Homburg, Germany.
Richard ZimmermannDepartment of Medical Biochemistry and Molecular Biology, Saarland University, D-66424 Homburg, Germany.
Grazia TammaDepartment of Biosciences, Biotechnologies and Biopharmaceutics, University of Bari, 70121 Bari, Italy.
Joseph Roman CaseyDepartment of Biochemistry, University of Alberta, Edmonton, AB T6G 1C9, Canada Department of Physiology, University of Alberta, Edmonton, AB T6G 1C9, Canada Membrane Protein Disease Research Group, University of Alberta, Edmonton, AB T6G 1C9, Canada.
Robert Todd AlexanderDepartment of Physiology, University of Alberta, Edmonton, AB T6G 1C9, Canada Membrane Protein Disease Research Group, University of Alberta, Edmonton, AB T6G 1C9, Canada Department of Pediatrics, University of Alberta, Edmonton, AB T6G 1C9, Canada todd2@ualberta.ca.
University of Alberta · CAUniversity of Bari Aldo Moro · ITSaarland University · DE

Funding

CIHR 106464-1CIHR 106464-2CIHR 136891-1CIHR 96175-1CIHR 96175-2
6 · The paper itself

Abstract

Aquaporin-1 (AQP1) enables greatly enhanced water flux across plasma membranes. The cytosolic carboxy terminus of AQP1 has two acidic motifs homologous to known carbonic anhydrase II (CAII) binding sequences. CAII colocalizes with AQP1 in the renal proximal tubule. Expression of AQP1 with CAII in Xenopus oocytes or mammalian cells increased water flux relative to AQP1 expression alone. This required the amino-terminal sequence of CAII, a region that binds other transport proteins. Expression of catalytically inactive CAII failed to increase water flux through AQP1. Proximity ligation assays revealed close association of CAII and AQP1, an effect requiring the second acidic cluster of AQP1. This motif was also necessary for CAII to increase AQP1-mediated water flux. Red blood cell ghosts resealed with CAII demonstrated increased osmotic water permeability compared with ghosts resealed with albumin. Water flux across renal cortical membrane vesicles, measured by stopped-flow light scattering, was reduced in CAII-deficient mice compared with wild-type mice. These data are consistent with CAII increasing water conductance through AQP1 by a physical interaction between the two proteins.

Indexed as

Amino Acid SequenceAnimalsAquaporin 1Carbonic Anhydrase IICell Membrane PermeabilityCells, CulturedErythrocytesHEK293 CellsHumansMolecular Sequence DataProtein BindingProtein Interaction MappingWaterXenopus laevisAQP1 protein, humanAquaporin 1Carbonic Anhydrase IIWater

Identifiers

PMID25609088
PMCPMC4357510
OpenAlexW2122142201

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.