Evidence map›Paper›PMID 25644708›Full record

ArticleMolecular microbiology2015

LiZIP3 is a cellular zinc transporter that mediates the tightly regulated import of zinc in Leishmania infantum parasites.

Sandra Carvalho, Rosa Barreira da Silva, Ali Shawki, Helena Castro, Márcia Lamy, David Eide, Vítor Costa, Bryan Mackenzie, Ana M Tomás

Open access · bronzeAbstract read
In one paragraph

Article in Molecular microbiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
2.0field-weighted citation impact, top 16% 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

13 citing papers in PubMed, 19 citations in OpenAlex.

  1. Article
  2. Article
  3. Identification ofFrontiers in cellular and infection microbiology · 2022
    Article
  4. Article
  5. Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  6. Article
  7. Review
  8. Article
  9. The role of zinc and its compounds in leukemia.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2018
    Review
  10. Pan-Domain Analysis of ZIP Zinc Transporters.International journal of molecular sciences · 2017
    Review
  11. Article
  12. Article
  13. 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

9 authors at 4 institutions in 2 countries.

Sandra CarvalhoInstituto de Investigação e Inovação em Saúde, Universidade do Porto, Porto, 4200, Portugal; IBMC - Instituto de Biologia Molecular e Celular, Universidade do Porto, Porto, 4150-180, Portugal; ICBAS - Instituto de Ciências Biomédicas Abel Salazar, Universidade do Porto, Porto, 4050-313, Portugal.
Rosa Barreira da Silva
Ali Shawki
Helena Castro
Márcia Lamy
David Eide
Vítor Costa
Bryan Mackenzie
Ana M Tomás
i3S - Instituto de Investigação e Inovação em Saúde, Universidade do Porto · PTUniversidade do Porto · PTUniversity of Cincinnati Medical Center · USUniversity of Wisconsin–Madison · US

Funding

REGULATION OF CELLULAR ZINC HOMEOSTASISR01GM056285 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI EIDE, DAVID J · 1997 to 2022
$6.2M
Divalent metal-ion transporter DMT1 and its role in intestinal metal-ion uptakeR01DK080047 · NIDDK · UNIVERSITY OF CINCINNATI · PI MACKENZIE, BRYAN · 2008 to 2012
$1.5M
NIDDK NIH HHS R01 DK080047NIGMS NIH HHS R01 GM056285NIGMS NIH HHS R01 GM56285
6 · The paper itself

Abstract

Cellular zinc homeostasis ensures that the intracellular concentration of this element is kept within limits that enable its participation in critical physiological processes without exerting toxic effects. We report here the identification and characterization of the first mediator of zinc homeostasis in Leishmania infantum, LiZIP3, a member of the ZIP family of divalent metal-ion transporters. The zinc transporter activity of LiZIP3 was first disclosed by its capacity to rescue the growth of Saccharomyces cerevisiae strains deficient in zinc acquisition. Subsequent expression of LiZIP3 in Xenopus laevis oocytes was shown to stimulate the uptake of a broad range of metal ions, among which Zn(2+) was the preferred LiZIP3 substrate (K0.5  ≈ 0.1 μM). Evidence that LiZIP3 functions as a zinc importer in L. infantum came from the observations that the protein locates to the cell membrane and that its overexpression leads to augmented zinc internalization. Importantly, expression and cell-surface location of LiZIP3 are lost when parasites face high zinc bioavailability. LiZIP3 decline in response to zinc is regulated at the mRNA level in a process involving (a) short-lived protein(s). Collectively, our data reveal that LiZIP3 enables L. infantum to acquire zinc in a highly regulated manner, hence contributing to zinc homeostasis.

Indexed as

AnimalsCarrier ProteinsGene Expression ProfilingGenetic Complementation TestLeishmania infantumOocytesProtozoan ProteinsSaccharomyces cerevisiaeSubstrate SpecificityXenopus laevisZincCarrier ProteinsProtozoan ProteinsZinczinc-binding protein

Identifiers

PMID25644708
PMCPMC4964273
OpenAlexW1937293045

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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.