Evidence map›Paper›PMID 36454509›Full record

ArticleBiometals : an international journal on the role of metal ions in biology, biochemistry, and medicine2023

Functional characterization of SLC39 family members ZIP5 and ZIP10 in overexpressing HEK293 cells reveals selective copper transport activity.

Marcello Polesel, Alvaro Ingles-Prieto, Eirini Christodoulaki, Evandro Ferrada, Cédric Doucerain, Patrick Altermatt, Michelle Knecht, Michael Kuhn, Anna-Lena Steck, Maria Wilhelm and 1 more

Erratum issuedOpen access · hybridAbstract read
In one paragraph

Article in Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine, 2023. 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 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
3.2field-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

14 citing papers in PubMed, 29 citations in OpenAlex.

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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

11 authors at 2 institutions in 2 countries.

Marcello Polesel *Vifor (International) AG, Wagistrasse 27a, 8952, Schlieren, Switzerland. marcello.polesel@viforpharma.com.ORCID http://orcid.org/0000-0003-0668-8099
Alvaro Ingles-Prieto *CeMM Research Center for Molecular Medicine of the Austrian Academy of Sciences, Lazarettgasse 14, 1090, Vienna, Austria.ORCID http://orcid.org/0000-0002-5409-8571
Eirini ChristodoulakiCeMM Research Center for Molecular Medicine of the Austrian Academy of Sciences, Lazarettgasse 14, 1090, Vienna, Austria.ORCID http://orcid.org/0000-0001-9834-1257
Evandro FerradaCeMM Research Center for Molecular Medicine of the Austrian Academy of Sciences, Lazarettgasse 14, 1090, Vienna, Austria.ORCID http://orcid.org/0000-0003-3242-1726
Cédric DoucerainVifor (International) AG, Wagistrasse 27a, 8952, Schlieren, Switzerland.
Patrick AltermattVifor (International) AG, Wagistrasse 27a, 8952, Schlieren, Switzerland.
Michelle KnechtVifor (International) AG, Wagistrasse 27a, 8952, Schlieren, Switzerland.
Michael KuhnVifor (International) AG, Wagistrasse 27a, 8952, Schlieren, Switzerland.
Anna-Lena SteckVifor (International) AG, Wagistrasse 27a, 8952, Schlieren, Switzerland.
Maria WilhelmVifor (International) AG, Wagistrasse 27a, 8952, Schlieren, Switzerland.
Vania ManolovaVifor (International) AG, Wagistrasse 27a, 8952, Schlieren, Switzerland.
Vifor Pharma (Switzerland) · CHAustrian Academy of Sciences · AT

Funding

Innovative Medicines Initiative 2 Joint Undertaking 777372
6 · The paper itself

Abstract

Zinc is the second most prevalent metal element present in living organisms, and control of its concentration is pivotal to physiology. The amount of zinc available to the cell cytoplasm is regulated by the activity of members of the SLC39 family, the ZIP proteins. Selectivity of ZIP transporters has been the focus of earlier studies which provided a biochemical and structural basis for the selectivity for zinc over other metals such as copper, iron, and manganese. However, several previous studies have shown how certain ZIP proteins exhibit higher selectivity for metal elements other than zinc. Sequence similarities suggest an evolutionary basis for the elemental selectivity within the ZIP family. Here, by engineering HEK293 cells to overexpress ZIP proteins, we have studied the selectivity of two phylogenetic clades of ZIP proteins, that is ZIP8/ZIP14 (previously known to be iron and manganese transporters) and ZIP5/ZIP10. By incubating ZIP over-expressing cells in presence of several divalent metals, we found that ZIP5 and ZIP10 are high affinity copper transporters with greater selectivity over other elements, revealing a novel substrate signature for the ZIP5/ZIP10 clade.

Indexed as

CopperManganeseCation Transport ProteinsHEK293 CellsHumansIronMembrane Transport ProteinsMetalsPhylogenyZincCation Transport ProteinsCopperIronManganeseMembrane Transport ProteinsMetalsSLC39A10 protein, humanZincICP-MSIonomicsSLC39A10SLC39A5ZIP10ZIP5

Identifiers

PMID36454509
PMCPMC11196296
OpenAlexW4310567959

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Registered trials

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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.