Evidence map›Paper›PMID 24367080›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2014

Heteromerization of PIP aquaporins affects their intrinsic permeability.

Agustín Yaneff, Lorena Sigaut, Mercedes Marquez, Karina Alleva, Lía Isabel Pietrasanta, Gabriela Amodeo

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing papers in PubMed
4.2field-weighted citation impact, top 5% 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

57 citing papers in PubMed, 115 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Aquaporin Modulation by Cations, a Review.Current issues in molecular biology · 2024
    Review
  11. Article
  12. Article
  13. PbHsfC1a-coordinates ABA biosynthesis and HPlant biotechnology journal · 2024
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Mechanosensitive aquaporins.Biophysical reviews · 2023
    Review
  20. Fifty years of biophysics in Argentina.Biophysical reviews · 2023
    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

6 authors at 3 institutions in 1 country.

Agustín YaneffInstituto de Biodiversidad y Biología Experimental and Departamento de Biodiversidad y Biología Experimental, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, C1428EHA Buenos Aires, Argentina.
Lorena Sigaut
Mercedes Marquez
Karina Alleva
Lía Isabel Pietrasanta
Gabriela Amodeo
University of Buenos Aires · ARCentro Científico Tecnológico - San Juan · ARFundación Ciencias Exactas y Naturales · AR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The plant aquaporin plasma membrane intrinsic proteins (PIP) subfamily represents one of the main gateways for water exchange at the plasma membrane (PM). A fraction of this subfamily, known as PIP1, does not reach the PM unless they are coexpressed with a PIP2 aquaporin. Although ubiquitous and abundantly expressed, the role and properties of PIP1 aquaporins have therefore remained masked. Here, we unravel how FaPIP1;1, a fruit-specific PIP1 aquaporin from Fragaria x ananassa, contributes to the modulation of membrane water permeability (Pf) and pH aquaporin regulation. Our approach was to combine an experimental and mathematical model design to test its activity without affecting its trafficking dynamics. We demonstrate that FaPIP1;1 has a high water channel activity when coexpressed as well as how PIP1-PIP2 affects gating sensitivity in terms of cytosolic acidification. PIP1-PIP2 random heterotetramerization not only allows FaPIP1;1 to arrive at the PM but also produces an enhancement of FaPIP2;1 activity. In this context, we propose that FaPIP1;1 is a key participant in the regulation of water movement across the membranes of cells expressing both aquaporins.

Indexed as

Gene Expression Regulation, PlantAnimalsAquaporinsBacterial ProteinsCell MembraneCytosolFragariaHydrogen-Ion ConcentrationLipid BilayersLuminescent ProteinsMicroscopy, ConfocalModels, TheoreticalMutagenesis, Site-DirectedOocytesPermeabilityPlant ProteinsAquaporinsBacterial ProteinsLipid BilayersLuminescent Proteinsmajor intrinsic protein, plantPlant ProteinsRNA, ComplementaryWateryellow fluorescent protein, Bacteria

Identifiers

PMID24367080
PMCPMC3890845
OpenAlexW2032067567

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.