Evidence map›Paper›PMID 22865877›Full record

ArticleThe Journal of biological chemistry2012

COPT6 is a plasma membrane transporter that functions in copper homeostasis in Arabidopsis and is a novel target of SQUAMOSA promoter-binding protein-like 7.

Ha-il Jung, Sheena R Gayomba, Michael A Rutzke, Eric Craft, Leon V Kochian, Olena K Vatamaniuk

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
8.9field-weighted citation impact, top 2% 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

39 citing papers in PubMed, 107 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Review
  5. Article
  6. Review
  7. Article
  8. Article
  9. Physiological and Molecular Mechanisms of Plant Responses to Copper Stress.International journal of molecular sciences · 2022
    Review
  10. TheInternational journal of molecular sciences · 2022
    Article
  11. Article
  12. CITF1 Functions Downstream of SPL7 to Specifically Regulate Cu Uptake inInternational journal of molecular sciences · 2022
    Article
  13. Review
  14. Article
  15. Copper: uptake, toxicity and tolerance in plants and management of Cu-contaminated soil.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2021
    Review
  16. Article
  17. Article
  18. Review
  19. Article
  20. Characterization of the Copper Transporters fromInternational journal of molecular sciences · 2019
    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.

Ha-il JungDepartment of Crop and Soil Sciences, Cornell University, Ithaca, New York 14853, USA.
Sheena R Gayomba
Michael A Rutzke
Eric Craft
Leon V Kochian
Olena K Vatamaniuk
Cornell University · USUnited States Department of Agriculture · USRobert W. Holley Center for Agriculture & Health · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Among the mechanisms controlling copper homeostasis in plants is the regulation of its uptake and tissue partitioning. Here we characterized a newly identified member of the conserved CTR/COPT family of copper transporters in Arabidopsis thaliana, COPT6. We showed that COPT6 resides at the plasma membrane and mediates copper accumulation when expressed in the Saccharomyces cerevisiae copper uptake mutant. Although the primary sequence of COPT6 contains the family conserved domains, including methionine-rich motifs in the extracellular N-terminal domain and a second transmembrane helix (TM2), it is different from the founding family member, S. cerevisiae Ctr1p. This conclusion was based on the finding that although the positionally conserved Met(106) residue in the TM2 of COPT6 is functionally essential, the conserved Met(27) in the N-terminal domain is not. Structure-function studies revealed that the N-terminal domain is dispensable for COPT6 function in copper-replete conditions but is important under copper-limiting conditions. In addition, COPT6 interacts with itself and with its homolog, COPT1, unlike Ctr1p, which interacts only with itself. Analyses of the expression pattern showed that although COPT6 is expressed in different cell types of different plant organs, the bulk of its expression is located in the vasculature. We also show that COPT6 expression is regulated by copper availability that, in part, is controlled by a master regulator of copper homeostasis, SPL7. Finally, studies using the A. thaliana copt6-1 mutant and plants overexpressing COPT6 revealed its essential role during copper limitation and excess.

Indexed as

Promoter Regions, GeneticArabidopsisArabidopsis ProteinsBiological TransportCell MembraneCopper Transporter 1DNA-Binding ProteinsGene Expression Regulation, PlantGenetic Complementation TestHomeostasisMembrane Transport ProteinsMicroscopy, ConfocalMutagenesis, Site-DirectedPlants, Genetically ModifiedSLC31 ProteinsTranscription FactorsArabidopsis ProteinsCopper Transporter 1COPT1 protein, ArabidopsisCOPT6 protein, ArabidopsisDNA-Binding ProteinsMembrane Transport ProteinsSLC31 ProteinsSPL7 protein, ArabidopsisTranscription Factors

Identifiers

PMID22865877
PMCPMC3460430
OpenAlexW1985685584

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.