Evidence map›Paper›PMID 19636075›Full record

ArticleThe Journal of biological chemistry2009

ATP binding to the C terminus of the Arabidopsis thaliana nitrate/proton antiporter, AtCLCa, regulates nitrate transport into plant vacuoles.

Alexis De Angeli, Oscar Moran, Stefanie Wege, Sophie Filleur, Geneviève Ephritikhine, Sébastien Thomine, Hélène Barbier-Brygoo, Franco Gambale

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
13.5field-weighted citation impact, top 1% 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

43 citing papers in PubMed, 80 citations in OpenAlex.

  1. Review
  2. The Maize ZmbHLH118 Transcription Factor Regulates Vacuolar Nitrate Loading by the NOAdvanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  3. Homeostasis of ammonium and nitrate in plants.Quantitative plant biology · 2026
    Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. Review
  9. Article
  10. Article
  11. Review
  12. Chromophorylation of cyanobacteriochrome Slr1393 fromThe Journal of biological chemistry · 2018
    Article
  13. ATP-dependent modulation of MgtE in MgNature communications · 2017
    Article
  14. Review
  15. Review
  16. Review
  17. Article
  18. Article
  19. Article
  20. 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

8 authors at 3 institutions in 2 countries.

Alexis De AngeliIstituto di Biofisica, Consiglio Nazionale delle Ricerche, 16149 Genova, Italy.
Oscar Moran
Stefanie Wege
Sophie Filleur
Geneviève Ephritikhine
Sébastien Thomine
Hélène Barbier-Brygoo
Franco Gambale
Institut des Sciences du Végétal · FRCentre National de la Recherche Scientifique · FRInstituto Biofisika · ES

Funding

Catalytic mechanism of F1Fo-ATP synthaseR01GM071462 · NIGMS · TEXAS TECH UNIVERSITY · PI WEBER, JOACHIM · 2004 to 2010
$1.2M
NIGMS NIH HHS GM071462
6 · The paper itself

Abstract

Nitrate, one of the major nitrogen sources for plants, is stored in the vacuole. Nitrate accumulation within the vacuole is primarily mediated by the NO(3)(-)/H(+) exchanger AtCLCa, which belongs to the chloride channel (CLC) family. Crystallography analysis of hCLC5 suggested that the C-terminal domain, composed by two cystathionine beta-synthetase motifs in all eukaryotic members of the CLC family is able to interact with ATP. However, interaction of nucleotides with a functional CLC protein has not been unambiguously demonstrated. Here we show that ATP reversibly inhibits AtCLCa by interacting with the C-terminal domain. Applying the patch clamp technique to isolated Arabidopsis thaliana vacuoles, we demonstrate that ATP reduces AtCLCa activity with a maximum inhibition of 60%. ATP inhibition of nitrate influx into the vacuole at cytosolic physiological nitrate concentrations suggests that ATP modulation is physiologically relevant. ADP and AMP do not decrease the AtCLCa transport activity; nonetheless, AMP (but not ADP) competes with ATP, preventing inhibition. A molecular model of the C terminus of AtCLCa was built by homology to hCLC5 C terminus. The model predicted the effects of mutations of the ATP binding site on the interaction energy between ATP and AtCLCa that were further confirmed by functional expression of site-directed mutated AtCLCa.

Indexed as

Adenosine DiphosphateAdenosine MonophosphateAdenosine TriphosphateAlgorithmsAmino Acid SequenceArabidopsis ProteinsBinding SitesChloride ChannelsDose-Response Relationship, DrugIon TransportKineticsMembrane PotentialsModels, MolecularMolecular Sequence DataNitratesProtein BindingAdenosine DiphosphateAdenosine MonophosphateAdenosine TriphosphateArabidopsis ProteinsATCLC-A protein, ArabidopsisChloride ChannelsNitrates

Identifiers

PMID19636075
PMCPMC2785341
OpenAlexW2102947984

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.