Evidence map›Paper›PMID 24634212›Full record

ArticleThe Journal of biological chemistry2014

Uncoupling of ionic currents from substrate transport in the plant ammonium transporter AtAMT1;2.

Benjamin Neuhäuser, Uwe Ludewig

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
3.3field-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

14 citing papers in PubMed, 25 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Regulation of Cytosolic pH: The Contributions of Plant Plasma Membrane HInternational journal of molecular sciences · 2021
    Review
  5. Review
  6. Ammonium transporter expression in sperm of the disease vectorProceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  7. Function and Regulation of Ammonium Transporters in Plants.International journal of molecular sciences · 2020
    Review
  8. Functional Characterization of theFrontiers in plant science · 2020
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. 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

2 authors at 1 institution in 1 country.

Benjamin NeuhäuserInstitute of Crop Science, Nutritional Crop Physiology, University of Hohenheim, Fruwirthstrasse 20, D-70593 Stuttgart, Germany. Electronic address: benjamin.neuhaeuser@uni-hohenheim.de.
Uwe LudewigInstitute of Crop Science, Nutritional Crop Physiology, University of Hohenheim, Fruwirthstrasse 20, D-70593 Stuttgart, Germany.
University of Hohenheim · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The ammonium flux across prokaryotic, plant, and animal membranes is regulated by structurally related ammonium transporters (AMT) and/or related Rhesus (Rh) glycoproteins. Several plant AMT homologs, such as AtAMT1;2 from Arabidopsis, elicit ionic, ammonium-dependent currents when expressed in oocytes. By contrast, functional evidence for the transport of NH3 and the lack of coupled ionic currents has been provided for many Rh proteins. Furthermore, despite high resolution structures the transported substrate in many bacterial homologs, such as AmtB from Escherichia coli, is still unclear. In a heterologous genetic screen in yeast, AtAMT1;2 mutants with reduced transport activity were identified based on the resistance of yeast to the toxic transport analog methylamine. When expressed in oocytes, the reduced transport capacity was confirmed for either of the mutants Q67K, M72I,and W145S. Structural alignments suggest that these mutations were dispersed at subunit contact sites of trimeric AMTs, without direct contact to the pore lumen. Surprisingly, and in contrast to the wild type AtAMT1;2 transporter, ionic currents were not associated with the substrate transport in these mutants. Whether these data suggest that the wild type AtAMT1;2 functions as H(+)/NH3 co-transporter, as well as how the strict substrate coupling with protons is lost by the mutations, is discussed.

Indexed as

ArabidopsisCation Transport ProteinsIon ChannelsModels, MolecularMutationPlant Proteinsammonium transporters, plantCation Transport ProteinsIon ChannelsPlant ProteinsAmmoniaElectrophysiologyMembrane TransportPlantProton Transport

Identifiers

PMID24634212
PMCPMC4002075
OpenAlexW2100672176

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.