Evidence map›Paper›PMID 26780187›Full record

ArticleeLife2016

The magnesium transporter A is activated by cardiolipin and is highly sensitive to free magnesium in vitro.

Saranya Subramani, Harmonie Perdreau-Dahl, Jens Preben Morth

Open access · goldAbstract read
In one paragraph

Article in eLife, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
4.0field-weighted citation impact, top 7% 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

28 citing papers in PubMed, 56 citations in OpenAlex.

  1. Article
  2. Distinctive Lacritin Cleavage-Potentiated Bactericidal Alteration of thebioRxiv : the preprint server for biology · 2026
    Article
  3. Article
  4. Article
  5. Review
  6. ARNA (New York, N.Y.) · 2026
    Article
  7. P-type ATPase magnesium transporter MgtA acts as a dimer.Nature structural & molecular biology · 2025
    Article
  8. Article
  9. Review
  10. Article
  11. Review
  12. Article
  13. Article
  14. Reconsidering theACS bio & med chem Au · 2022
    Article
  15. Article
  16. Iron-responsive riboswitches.Current opinion in chemical biology · 2022
    Review
  17. Article
  18. Article
  19. Article
  20. 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

3 authors at 2 institutions in 1 country.

Saranya SubramaniNorwegian Centre of Molecular Medicine, Nordic EMBL Partnership University of Oslo, Oslo, Norway.
Harmonie Perdreau-DahlNorwegian Centre of Molecular Medicine, Nordic EMBL Partnership University of Oslo, Oslo, Norway.
Jens Preben MorthNorwegian Centre of Molecular Medicine, Nordic EMBL Partnership University of Oslo, Oslo, Norway.ORCID http://orcid.org/0000-0003-4077-0192
Oslo University Hospital · NOUniversity of Oslo · NO

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The magnesium transporter A (MgtA) is a specialized P-type ATPase, believed to import Mg(2+) into the cytoplasm. In Salmonella typhimurium and Escherichia coli, the virulence determining two-component system PhoQ/PhoP regulates the transcription of mgtA gene by sensing Mg(2+) concentrations in the periplasm. However, the factors that affect MgtA function are not known. This study demonstrates, for the first time, that MgtA is highly dependent on anionic phospholipids and in particular, cardiolipin. Colocalization studies confirm that MgtA is found in the cardiolipin lipid domains in the membrane. The head group of cardiolipin plays major role in activation of MgtA suggesting that cardiolipin may act as a Mg(2+) chaperone for MgtA. We further show that MgtA is highly sensitive to free Mg(2+) (Mg(2+)free) levels in the solution. MgtA is activated when the Mg(2+)free concentration is reduced below 10 μM and is strongly inhibited above 1 mM, indicating that Mg(2+)free acts as product inhibitor. Combined, our findings conclude that MgtA may act as a sensor as well as a transporter of Mg(2+).

Indexed as

Adenosine TriphosphatasesCardiolipinsCell MembraneEscherichia coliEscherichia coli ProteinsMagnesiumMembrane Transport ProteinsAdenosine TriphosphatasesCardiolipinsEscherichia coli ProteinsMagnesiumMembrane Transport ProteinsMgtA protein, E coliATPase assaybiochemistrybiophysicscardiolipinE. colimagnesium inhibitionmagnesium transportMgtAP-type ATPasestructural biology

Identifiers

PMID26780187
PMCPMC4758953
OpenAlexW2293349942

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.