Evidence map›Paper›PMID 16446503›Full record

ArticleThe Journal of general physiology2006

Different transport mechanisms in plant and human AMT/Rh-type ammonium transporters.

Maria Mayer, Gabriel Schaaf, Isabelle Mouro, Claude Lopez, Yves Colin, Petra Neumann, Jean-Pierre Cartron, Uwe Ludewig

Erratum issuedOpen access · bronzeAbstract readComparative Study
In one paragraph

Article in The Journal of general physiology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
5.4field-weighted citation impact, top 3% 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

42 citing papers in PubMed, 94 citations in OpenAlex.

  1. Rapid Visual Detection ofPlants (Basel, Switzerland) · 2024
    Article
  2. Review
  3. Ammonium transporter expression in sperm of the disease vectorProceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  4. Function and Regulation of Ammonium Transporters in Plants.International journal of molecular sciences · 2020
    Review
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Ammonia transport in the kidney by Rhesus glycoproteins.American journal of physiology. Renal physiology · 2014
    Review
  15. Article
  16. Review
  17. Article
  18. Article
  19. Renal ammonia metabolism and transport.Comprehensive Physiology · 2013
    Review
  20. Article
4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

8 authors at 2 institutions in 2 countries.

Maria MayerZentrum für Molekularbiologie der Pflanzen, Pflanzenphysiologie, Universität Tübingen, Tübingen, Germany.
Gabriel Schaaf
Isabelle Mouro
Claude Lopez
Yves Colin
Petra Neumann
Jean-Pierre Cartron
Uwe Ludewig
Inserm · FRUniversity of Tübingen · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The conserved family of AMT/Rh proteins facilitates ammonium transport across animal, plant, and microbial membranes. A bacterial homologue, AmtB, forms a channel-like structure and appears to function as an NH3 gas channel. To evaluate the function of eukaryotic homologues, the human RhCG glycoprotein and the tomato plant ammonium transporter LeAMT1;2 were expressed and compared in Xenopus oocytes and yeast. RhCG mediated the electroneutral transport of methylammonium (MeA), which saturated with Km = 3.8 mM at pHo 7.5. Uptake was strongly favored by increasing the pHo and was inhibited by ammonium. Ammonium induced rapid cytosolic alkalinization in RhCG-expressing oocytes. Additionally, RhCG expression was associated with an alkali-cation conductance, which was not significantly permeable to NH4+ and was apparently uncoupled from the ammonium transport. In contrast, expression of the homologous LeAMT1;2 induced pHo-independent MeA+ uptake and specific NH4+ and MeA+ currents that were distinct from endogenous currents. The different mechanisms of transport, including the RhCG-associated alkali-cation conductance, were verified by heterologous expression in appropriate yeast strains. Thus, homologous AMT/Rh-type proteins function in a distinct manner; while LeAMT1;2 carries specifically NH4+, or cotransports NH3/H+, RhCG mediates electroneutral NH3 transport.

Indexed as

AmmoniaAnimalsCation Transport ProteinsFemaleHumansHydrogen-Ion ConcentrationIon TransportMembrane GlycoproteinsMembrane PotentialsMethylaminesOocytesPatch-Clamp TechniquesPlant ProteinsQuaternary Ammonium CompoundsSaccharomyces cerevisiaeSolanum lycopersicumAmmoniaammonium transporters, plantCation Transport ProteinsMembrane GlycoproteinsmethylamineMethylaminesPlant ProteinsQuaternary Ammonium CompoundsRHCG protein, human

Identifiers

PMID16446503
PMCPMC2151487
OpenAlexW2144737544

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.